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  1 / 106522 MEDLINE  
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[PMID]:29172693
[Au] Autor:Ojeda-Montes MJ; Ardid-Ruiz A; Tomás-Hernández S; Gimeno A; Cereto-Massagué A; Beltrán-Debón R; Mulero M; Garcia-Vallvé S; Pujadas G; Valls C
[Ad] Endereço:Research group in Cheminformatics & Nutrition, Departament de Bioquímica i Biotecnologia, Universitat Rovira i Virgili, Campus de Sescelades, Tarragona, Catalonia 43007, Spain.
[Ti] Título:Ephedrine as a lead compound for the development of new DPP-IV inhibitors.
[So] Source:Future Med Chem;9(18):2129-2146, 2017 12.
[Is] ISSN:1756-8927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIM: Extracts from Ephedra species have been reported to be effective as antidiabetics. A previous in silico study predicted that ephedrine and five ephedrine derivatives could contribute to the described antidiabetic effect of Ephedra extracts by inhibiting dipeptidyl peptidase IV (DPP-IV). Finding selective DPP-IV inhibitors is a current therapeutic strategy for Type 2 diabetes mellitus management. Therefore, the main aim of this work is to experimentally determine whether these alkaloids are DPP-IV inhibitors. Materials & methods: The DPP-IV inhibition of Ephedra's alkaloids was determined via a competitive-binding assay. Then, computational analyses were used in order to find out the protein-ligand interactions and to perform a lead optimization. RESULTS: Our results show that all six molecules are DPP-IV inhibitors, with IC ranging from 124 µM for ephedrine to 28 mM for N-methylpseudoephedrine. CONCLUSION: Further computational analysis shows how Ephedra's alkaloids could be used as promising lead molecules for designing more potent and selective DPP-IV inhibitors.
[Mh] Termos MeSH primário: Dipeptidil Peptidase 4/metabolismo
Inibidores da Dipeptidil Peptidase IV/química
Efedrina/análogos & derivados
Hipoglicemiantes/química
[Mh] Termos MeSH secundário: Alcaloides/química
Alcaloides/metabolismo
Sítios de Ligação
Ligação Competitiva
Dipeptidil Peptidase 4/química
Desenho de Drogas
Ephedra/química
Ephedra/metabolismo
Efedrina/metabolismo
Hipoglicemiantes/metabolismo
Concentração Inibidora 50
Simulação de Acoplamento Molecular
Fenilpropanolamina/química
Extratos Vegetais/química
Isoformas de Proteínas/antagonistas & inibidores
Isoformas de Proteínas/metabolismo
Estrutura Terciária de Proteína
Estereoisomerismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Alkaloids); 0 (Dipeptidyl-Peptidase IV Inhibitors); 0 (Hypoglycemic Agents); 0 (Plant Extracts); 0 (Protein Isoforms); 33RU150WUN (Phenylpropanolamine); EC 3.4.14.5 (Dipeptidyl Peptidase 4); GN83C131XS (Ephedrine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.4155/fmc-2017-0080


  2 / 106522 MEDLINE  
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[PMID]:29328338
[Au] Autor:Soler MA; Fortuna S; de Marco A; Laio A
[Ad] Endereço:SISSA, Via Bonomea 265, I-34136 Trieste, Italy. miguelangel.solerbastida@sissa.it fortuna@sissa.it.
[Ti] Título:Binding affinity prediction of nanobody-protein complexes by scoring of molecular dynamics trajectories.
[So] Source:Phys Chem Chem Phys;20(5):3438-3444, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nanobodies offer a viable alternative to antibodies for engineering high affinity binders. Their small size has an additional advantage: it allows exploiting computational protocols for optimizing their biophysical features, such as the binding affinity. The efficient prediction of this quantity is still considered a daunting task especially for modelled complexes. We show how molecular dynamics can successfully assist in the binding affinity prediction of modelled nanobody-protein complexes. The approximate initial configurations obtained by in silico design must undergo large rearrangements before achieving a stable conformation, in which the binding affinity can be meaningfully estimated. The scoring functions developed for the affinity evaluation of crystal structures will provide accurate estimates for modelled binding complexes if the scores are averaged over long finite temperature molecular dynamics simulations.
[Mh] Termos MeSH primário: Complexo Antígeno-Anticorpo/química
Simulação de Dinâmica Molecular
Proteínas/imunologia
Anticorpos de Cadeia Única/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Afinidade de Anticorpos
Complexo Antígeno-Anticorpo/metabolismo
Seres Humanos
Muramidase/química
Muramidase/imunologia
Estrutura Terciária de Proteína
Proteínas/química
Receptor ErbB-2/química
Receptor ErbB-2/metabolismo
Alinhamento de Sequência
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Proteins); 0 (Single-Chain Antibodies); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2); EC 3.2.1.17 (Muramidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp08116b


  3 / 106522 MEDLINE  
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[PMID]:28951254
[Au] Autor:Palanisamy N; Akaberi D; Lennerstrand J
[Ad] Endereço:Molecular and Cellular Engineering Group, BioQuant, University of Heidelberg, Heidelberg, Germany; The Hartmut Hoffmann-Berling International Graduate School of Molecular and Cellular Biology (HBIGS), University of Heidelberg, Heidelberg, Germany. Electronic address: navaneethan.palanisamy@bioquant.uni-heidelberg.de.
[Ti] Título:Protein backbone flexibility pattern is evolutionarily conserved in the Flaviviridae family: A case of NS3 protease in Flavivirus and Hepacivirus.
[So] Source:Mol Phylogenet Evol;118:58-63, 2018 Jan.
[Is] ISSN:1095-9513
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Viruses belonging to the Flaviviridae family have been an important health concern for humans, animals and birds alike. No specific treatment is available yet for many of the viral infections caused by the members of this family. Lack of specific drugs against these viruses is mainly due to lack of protein structure information. It has been known that protein backbone fluctuation pattern is highly conserved in protein pairs with similar folds, in spite of the lack of sequence similarity. We hypothesized that this concept should also hold true for proteins (especially enzymes) of viruses included in different genera of the Flaviviridae family, as we know that the sequence similarity between them is low. Using available NS3 protease crystal structures of the Flaviviridae family, our preliminary results have shown that the Cα (i.e. backbone) fluctuation patterns are highly similar between Flaviviruses and a Hepacivirus (i.e. hepatitis C virus, HCV). This has to be validated further experimentally.
[Mh] Termos MeSH primário: Evolução Molecular
Flavivirus/enzimologia
Hepacivirus/enzimologia
Proteínas não Estruturais Virais/classificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Seres Humanos
Funções Verossimilhança
Filogenia
Estrutura Terciária de Proteína
RNA Helicases/química
RNA Helicases/classificação
RNA Helicases/genética
Alinhamento de Sequência
Serina Endopeptidases/química
Serina Endopeptidases/classificação
Serina Endopeptidases/genética
Proteínas não Estruturais Virais/química
Proteínas não Estruturais Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NS3 protein, flavivirus); 0 (NS3 protein, hepatitis C virus); 0 (Viral Nonstructural Proteins); EC 3.4.21.- (Serine Endopeptidases); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170928
[St] Status:MEDLINE


  4 / 106522 MEDLINE  
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[PMID]:28468956
[Au] Autor:Jasnovidova O; Krejcikova M; Kubicek K; Stefl R
[Ad] Endereço:CEITEC - Central European Institute of Technology, Masaryk University, Brno, Czech Republic olga.jasnovidova@ceitec.muni.cz richard.stefl@ceitec.muni.cz.
[Ti] Título:Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p.
[So] Source:EMBO Rep;18(6):906-913, 2017 Jun.
[Is] ISSN:1469-3178
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phosphorylation patterns of the C-terminal domain (CTD) of largest subunit of RNA polymerase II (called the CTD code) orchestrate the recruitment of RNA processing and transcription factors. Recent studies showed that not only serines and tyrosines but also threonines of the CTD can be phosphorylated with a number of functional consequences, including the interaction with yeast transcription termination factor, Rtt103p. Here, we report the solution structure of the Rtt103p CTD-interacting domain (CID) bound to Thr4 phosphorylated CTD, a poorly understood letter of the CTD code. The structure reveals a direct recognition of the phospho-Thr4 mark by Rtt103p CID and extensive interactions involving residues from three repeats of the CTD heptad. Intriguingly, Rtt103p's CID binds equally well Thr4 and Ser2 phosphorylated CTD A doubly phosphorylated CTD at Ser2 and Thr4 diminishes its binding affinity due to electrostatic repulsion. Our structural data suggest that the recruitment of a CID-containing CTD-binding factor may be coded by more than one letter of the CTD code.
[Mh] Termos MeSH primário: RNA Polimerase II/química
Proteínas de Saccharomyces cerevisiae/química
Treonina/química
Fatores de Transcrição/química
[Mh] Termos MeSH secundário: Fosforilação
Ligação Proteica
Proteínas Quinases/metabolismo
Estrutura Terciária de Proteína
Proteólise
RNA Polimerase II/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Serina/metabolismo
Treonina/metabolismo
Fatores de Transcrição/metabolismo
Transcrição Genética
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Rtt103 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 2ZD004190S (Threonine); 42HK56048U (Tyrosine); 452VLY9402 (Serine); EC 2.7.- (Protein Kinases); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.15252/embr.201643723


  5 / 106522 MEDLINE  
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[PMID]:29304128
[Au] Autor:Wang M; Zhai L; Yu W; Wei Y; Wang L; Liu S; Li W; Li X; Yu S; Chen X; Zhang H; Chen J; Feng Z; Yu L; Cui Y
[Ad] Endereço:College of Life Science and Technology, Heilongjiang Bayi Agricultural University, Daqing, P.R. China.
[Ti] Título:Identification of a protective B-cell epitope of the Staphylococcus aureus GapC protein by screening a phage-displayed random peptide library.
[So] Source:PLoS One;13(1):e0190452, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The impact of epidemic Staphylococcus aureus (S. aureus) on public health is increasing. Because of the abuse of antibiotics, the antibiotic resistance of S. aureus is increasing. Thus, there is an urgent need to develop new immunotherapies and immunoprophylaxes. Previous studies showed that the GapC protein of S. aureus, which is a surface protein with high glyceraldehyde 3-phosphate dehydrogenase activity, transferrin binding activity, and other biological activities, is highly conserved. GapC induces an effective humoral immune response in vivo. However, the B-cell epitopes of S. aureus GapC have not been well identified. Here we used the bioinformatics tools to analyze the sequence of GapC, and we generated protective anti-GapC monoclonal antibodies (mAbs). A protective mAb (1F4) showed strong specificity to GapC and the ability to induce macrophages to phagocytose S. aureus. We screened the motif 272GYTEDEIVSSD282, which was recognized by mAb 1F4, using a phage display system. Then, we used site-directed mutagenesis to identify key amino acids in the motif. Residues G272 D276 E277 I278 and V279 formed the core of the 272GYTEDEIVSSD282 motif. In addition, we showed that this epitope peptide induced a protective humoral immune response against S. aureus infection in immunized mice. Our results will be useful for the further study of epitope-based vaccines against S. aureus infection.
[Mh] Termos MeSH primário: Anticorpos Antibacterianos/imunologia
Antígenos de Bactérias/imunologia
Linfócitos B/imunologia
Proteínas de Bactérias/imunologia
Bacteriófagos/genética
Epitopos/imunologia
Biblioteca de Peptídeos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anticorpos Antibacterianos/biossíntese
Anticorpos Monoclonais/imunologia
Ensaio de Imunoadsorção Enzimática
Epitopos/química
Macrófagos/imunologia
Camundongos
Camundongos Endogâmicos BALB C
Mutagênese Sítio-Dirigida
Fagocitose
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Bacterial); 0 (Antibodies, Monoclonal); 0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (Epitopes); 0 (GapC protein, Streptococcus); 0 (Peptide Library)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190452


  6 / 106522 MEDLINE  
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[PMID]:29197270
[Au] Autor:Majiya H; Adeyemi OO; Stonehouse NJ; Millner P
[Ad] Endereço:School of Biomedical Sciences, University of Leeds, UK.
[Ti] Título:Photodynamic inactivation of bacteriophage MS2: The A-protein is the target of virus inactivation.
[So] Source:J Photochem Photobiol B;178:404-411, 2018 Jan.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Singlet oxygen mediated oxidation has been shown to be responsible for photodynamic inactivation (PDI) of viruses in solution with photosensitisers such as 5, 10, 15, 20-tetrakis (1-methyl-4-pyridinio) porphyrin tetra p-toluenesulfonate (TMPyP). The capsids of non-enveloped viruses, such as bacteriophage MS2, are possible targets for viral inactivation by singlet oxygen oxidation. Within the capsid (predominantly composed of coat protein), the A-protein acts as the host recognition and attachment protein. The A-protein has two domains; an α-helix domain and a ß-sheet domain. The α-helix domain is attached to the viral RNA genome inside the capsid while the ß-sheet domain, which is on the surface of the capsid, is believed to be the site for attachment to the host bacteria pilus during infection. In this study, 4 sequence-specific antibodies were raised against 4 sites on the A-protein. Changes induced by the oxidation of singlet oxygen were compared to the rate of PDI of the virus. Using these antibodies, our results suggest that the rate of PDI is relative to loss of antigenicity of two sites on the A-protein. Our data further showed that PDI caused aggregation of MS2 particles and crosslinking of MS2 coat protein. However, these inter- and intra-capsid changes did not correlate to the rate of PDI we observed in MS2. Possible modes of action are discussed as a means to gaining insight to the targets and mechanisms of PDI of viruses.
[Mh] Termos MeSH primário: Levivirus/fisiologia
Proteínas Virais/antagonistas & inibidores
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Anticorpos/imunologia
Luz
Fármacos Fotossensibilizantes/química
Fármacos Fotossensibilizantes/farmacologia
Porfirinas/química
Porfirinas/farmacologia
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Oxigênio Singlete/química
Oxigênio Singlete/toxicidade
Proteínas Virais/imunologia
Proteínas Virais/metabolismo
Inativação de Vírus/efeitos dos fármacos
Inativação de Vírus/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Photosensitizing Agents); 0 (Porphyrins); 0 (Viral Proteins); 0 (maturation protein, Enterobacterio phage MS2); 17778-80-2 (Singlet Oxygen); 38673-65-3 (tetra(4-N-methylpyridyl)porphine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171203
[St] Status:MEDLINE


  7 / 106522 MEDLINE  
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[PMID]:29188241
[Au] Autor:Mondal S; Chakraborty K; Bandyopadhyay S
[Ad] Endereço:Molecular Modeling Laboratory, Department of Chemistry, Indian Institute of Technology, Kharagpur-721302, India. sanjoy@chem.iitkgp.ernet.in.
[Ti] Título:Microscopic understanding of the conformational features of a protein-DNA complex.
[So] Source:Phys Chem Chem Phys;19(48):32459-32472, 2017 Dec 13.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein-DNA interactions play crucial roles in different biological processes. Binding of a protein to its target DNA is the key step at different stages of genetic activities. In this article, we have carried out atomistic molecular dynamics simulations to understand the microscopic conformational and dynamical features of the N-terminal domain of the λ-repressor protein and its operator DNA in their complexed state. The calculations revealed that the overall flexibility of the protein and the DNA components reduces due to complex formation. In particular, increased ordering of the DNA sugar rings bound to the protein is found to be associated with modified ring puckering. Attempts have been made to study the effect of complexation on the internal motions of the protein and the DNA components. It is demonstrated that the non-uniform ordering of the side chains of lysine residues in the consensus sequence leads to differential behavior of the two monomers of the homodimeric protein.
[Mh] Termos MeSH primário: DNA/metabolismo
Proteínas Repressoras/metabolismo
Proteínas Virais Reguladoras e Acessórias/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bacteriófago lambda/metabolismo
Sequência de Bases
Sítios de Ligação
DNA/química
Simulação de Dinâmica Molecular
Conformação de Ácido Nucleico
Ligação Proteica
Estrutura Terciária de Proteína
Proteínas Repressoras/química
Proteínas Virais Reguladoras e Acessórias/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Repressor Proteins); 0 (Viral Regulatory and Accessory Proteins); 0 (phage repressor proteins); 9007-49-2 (DNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp05161a


  8 / 106522 MEDLINE  
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[PMID]:29175602
[Au] Autor:Thangaraj M; Gengan RM; Ranjan B; Muthusamy R
[Ad] Endereço:Department of Chemistry, Faculty of Applied Sciences, Durban University of Technology, Durban 4001, South Africa.
[Ti] Título:Synthesis, molecular docking, antimicrobial, antioxidant and toxicity assessment of quinoline peptides.
[So] Source:J Photochem Photobiol B;178:287-295, 2018 Jan.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:A series of quinoline based peptides were synthesized by a one-pot reaction through Ugi-four component condensation of lipoic acid, cyclohexyl isocyanide, aniline derivatives and 2-methoxy quinoline-3-carbaldehyde derivatives under microwave irradiation. The products were obtained in excellent yields and high purity. Solvent optimization and the effect of microwave irradiation with various powers were also observed. All the synthesized compounds were characterized by FTIR, NMR spectral data and elemental analysis. A total of eight peptides were subjected to antimicrobial, antioxidant and toxicity evaluation. Among them, four peptides showed potential towards antibacterial screening with Bacillus cereus, Staphylococcus aureus, Escherichia coli, Enterococcus faecalis and Candida albicans, Candida utilis and three peptides showed antioxidant test positive (DPPH). Besides, toxicity of all the peptides were evaluated by using brine shrimp and it was observed that four peptides showed mortality rate less than 50% up to 48h. Molecular docking studies revealed that the higher binding affinity of the two peptides toward DNA gyrase than ciprofloxacin based on Libdock score. The described chemistry represents a facile tool to synthesize complex heterocycles of pharmaceutical relevance in a highly efficient and one-pot fashion. The advantages of this method are its green approach, inexpensive solvent, shorter reaction times and excellent yields.
[Mh] Termos MeSH primário: Anti-Infecciosos/síntese química
Antioxidantes/química
Simulação de Acoplamento Molecular
Peptídeos/química
Quinolinas/química
[Mh] Termos MeSH secundário: Animais
Anti-Infecciosos/química
Anti-Infecciosos/farmacologia
Artemia/efeitos dos fármacos
Artemia/crescimento & desenvolvimento
Bacillus cereus/efeitos dos fármacos
Sítios de Ligação
Candida/efeitos dos fármacos
DNA Girase/química
DNA Girase/metabolismo
Enterococcus faecalis/efeitos dos fármacos
Escherichia coli/efeitos dos fármacos
Testes de Sensibilidade Microbiana
Peptídeos/síntese química
Estrutura Terciária de Proteína
Staphylococcus aureus/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Antioxidants); 0 (Peptides); 0 (Quinolines); E66400VT9R (quinoline); EC 5.99.1.3 (DNA Gyrase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  9 / 106522 MEDLINE  
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[PMID]:28740983
[Au] Autor:Consentius P; Gohlke U; Loll B; Alings C; Heinemann U; Wahl MC; Risse T
[Ad] Endereço:Freie Universität Berlin, Institute of Chemistry and Biochemistry, Takustr. 3, 14195 Berlin, Germany. risse@chemie.fu-berlin.de.
[Ti] Título:Combining EPR spectroscopy and X-ray crystallography to elucidate the structure and dynamics of conformationally constrained spin labels in T4 lysozyme single crystals.
[So] Source:Phys Chem Chem Phys;19(31):20723-20734, 2017 Aug 09.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Electron paramagnetic resonance (EPR) spectroscopy in combination with site-directed spin labeling is used to investigate the structure and dynamics of conformationally constrained spin labels in T4 lysozyme single crystals. Within a single crystal, the oriented ensemble of spin bearing moieties results in a strong angle dependence of the EPR spectra. A quantitative description of the EPR spectra requires the determination of the unit cell orientation with respect to the sample tube and the orientation of the spin bearing moieties within the crystal lattice. Angle dependent EPR spectra were analyzed by line shape simulations using the stochastic Liouville equation approach developed by Freed and co-workers and an effective Hamiltonian approach. The gain in spectral information obtained from the EPR spectra of single crystalline samples taken at different frequencies, namely the X-band and Q-band, allows us to discriminate between motional models describing the spectra of isotropic solutions similarly well. In addition, it is shown that the angle dependent single crystal spectra allow us to identify two spin label rotamers with very similar side chain dynamics. These results demonstrate the utility of single crystal EPR spectroscopy in combination with spectral line shape simulation techniques to extract valuable dynamic information not readily available from the analysis of isotropic systems. In addition, it will be shown that the loss of electron density in high resolution diffraction experiments at room temperature does not allow us to conclude that there is significant structural disorder in the system.
[Mh] Termos MeSH primário: Bacteriófago T4/enzimologia
Muramidase/química
Proteínas Virais/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Espectroscopia de Ressonância de Spin Eletrônica
Ligações de Hidrogênio
Estrutura Terciária de Proteína
Marcadores de Spin
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Spin Labels); 0 (Viral Proteins); EC 3.2.1.17 (Muramidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp03144k


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[PMID]:29178645
[Au] Autor:Bizarro J; Meier UT
[Ad] Endereço:Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York, 10461.
[Ti] Título:Inherited SHQ1 mutations impair interaction with NAP57/dyskerin, a major target in dyskeratosis congenita.
[So] Source:Mol Genet Genomic Med;5(6):805-808, 2017 11.
[Is] ISSN:2324-9269
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The inherited bone marrow failure syndrome dyskeratosis congenita (DC) is most frequently caused by mutations in DKC1 (MIM# 300126), the gene encoding NAP57 (aka dyskerin). The typically missense mutations modulate the interaction of NAP57 with its chaperone SHQ1, but no DC mutations have been identified in SHQ1 (MIM# 613663). Here, we report on two compound heterozygous mutations in SHQ1 in a patient with a severe neurological disorder including cerebellar degeneration. METHODS: The SHQ1 mutations were identified by patient exome sequencing. The impact of the mutations was assessed in pulldown assays with recombinant NAP57. RESULTS: The SHQ1 mutations were the only set of mutations consistent with an autosomal recessive mode of inheritance. The mutations map to the SHQ1-NAP57 interface and impair the interaction of the recombinant SHQ1 variants with NAP57. CONCLUSION: Intrauterine growth retardation and the neurological phenotype of the patient are reminiscent of the severe clinical variant of DC, the Hoyeraal-Hreidarsson syndrome (HH). Hence, SHQ1 screening may be warranted in patients with inherited bone marrow failure syndromes.
[Mh] Termos MeSH primário: Proteínas de Transporte/genética
Disceratose Congênita/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Encéfalo/diagnóstico por imagem
Proteínas de Transporte/metabolismo
Análise Mutacional de DNA
Disceratose Congênita/diagnóstico
Seres Humanos
Lactente
Imagem por Ressonância Magnética
Masculino
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Linhagem
Polimorfismo de Nucleotídeo Único
Ligação Proteica
Estrutura Terciária de Proteína
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Sequenciamento Completo do Exoma
[Pt] Tipo de publicação:CASE REPORTS; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (NAP57); 0 (Nuclear Proteins); 0 (Recombinant Proteins); 0 (SHQ1 protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1002/mgg3.314



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