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  1 / 13049 MEDLINE  
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[PMID]:28449057
[Au] Autor:Schumacher MA; Zeng W; Findlay KC; Buttner MJ; Brennan RG; Tschowri N
[Ad] Endereço:Department of Biochemistry, Duke University School of Medicine, Durham, NC 27701, USA.
[Ti] Título:The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD2-(c-di-GMP)4 complex.
[So] Source:Nucleic Acids Res;45(11):6923-6933, 2017 Jun 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Streptomyces are ubiquitous soil bacteria that undergo a complex developmental transition coinciding with their production of antibiotics. This transition is controlled by binding of a novel tetrameric form of the second messenger, 3΄-5΄ cyclic diguanylic acid (c-di-GMP) to the master repressor, BldD. In all domains of life, nucleotide-based second messengers allow a rapid integration of external and internal signals into regulatory pathways that control cellular responses to changing conditions. c-di-GMP can assume alternative oligomeric states to effect different functions, binding to effector proteins as monomers, intercalated dimers or, uniquely in the case of BldD, as a tetramer. However, at physiological concentrations c-di-GMP is a monomer and little is known about how higher oligomeric complexes assemble on effector proteins and if intermediates in assembly pathways have regulatory significance. Here, we show that c-di-GMP binds BldD using an ordered, sequential mechanism and that BldD function necessitates the assembly of the BldD2-(c-di-GMP)4 complex.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
GMP Cíclico/análogos & derivados
Proteínas Repressoras/química
Streptomyces
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalografia por Raios X
GMP Cíclico/química
Ligações de Hidrogênio
Modelos Moleculares
Ligação Proteica
Domínios Proteicos
Estabilidade Proteica
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Repressor Proteins); 61093-23-0 (bis(3',5')-cyclic diguanylic acid); H2D2X058MU (Cyclic GMP)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx287


  2 / 13049 MEDLINE  
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[PMID]:28741733
[Au] Autor:Tsukamoto H; Yamagata Y; Ukai I; Takeuchi S; Okubo M; Kobayashi Y; Kozakai S; Kubota K; Numasaki M; Kanemitsu Y; Matsumoto Y; Tomioka Y
[Ad] Endereço:Laboratory of Oncology, Pharmacy Practice and Sciences, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
[Ti] Título:An inhibitory epitope of human Toll-like receptor 4 resides on leucine-rich repeat 13 and is recognized by a monoclonal antibody.
[So] Source:FEBS Lett;591(16):2406-2416, 2017 08.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lipopolysaccharide (LPS)-induced activation of Toll-like receptor 4 (TLR4) elicits the innate immune response and can trigger septic shock if excessive. Two antibodies (HT4 and HT52) inhibit LPS-induced human TLR4 activation via novel LPS binding-independent mechanisms. The HT52 epitope resides on leucine-rich repeat 2 (LRR2) and is a feature of many inhibitory antibodies; antigen specificity of HT4 does not reside in LRR2. Here, we identified an HT4 epitope on LRR13 located close to the TLR4 dimerization interface that plays a role in NFκB activation. HT4 and HT52 mutually enhanced TLR4 inhibition. LRR13 is a novel inhibitory epitope and may be useful for developing anti-TLR4 antibodies. Combination therapy with LRR2 and LRR13 may effectively inhibit TLR4 activation.
[Mh] Termos MeSH primário: Motivos de Aminoácidos
Anticorpos Monoclonais/imunologia
Epitopos/imunologia
Receptor 4 Toll-Like/química
Receptor 4 Toll-Like/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Seres Humanos
Lipopolissacarídeos/farmacologia
Camundongos
Multimerização Proteica
Estrutura Quaternária de Proteína
Receptor 4 Toll-Like/metabolismo
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Epitopes); 0 (Lipopolysaccharides); 0 (TLR4 protein, human); 0 (Toll-Like Receptor 4)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12768


  3 / 13049 MEDLINE  
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[PMID]:29368769
[Au] Autor:Malý P; Gardiner AT; Cogdell RJ; van Grondelle R; Mancal T
[Ad] Endereço:Department of Biophysics, Faculty of Sciences, Vrije Universiteit Amsterdam, De Boeleaan 1081, 1081HV Amsterdam, The Netherlands. p.maly@vu.nl.
[Ti] Título:Robust light harvesting by a noisy antenna.
[So] Source:Phys Chem Chem Phys;20(6):4360-4372, 2018 Feb 07.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Photosynthetic light harvesting can be very efficient in solar energy conversion while taking place in a highly disordered and noisy physiological environment. This efficiency is achieved by the ultrafast speed of the primary photosynthetic processes, which is enabled by a delicate interplay of quantum effects, thermodynamics and environmental noise. The primary processes take place in light-harvesting antennas built from pigments bound to a fluctuating protein scaffold. Here, we employ ultrafast single-molecule spectroscopy to follow fluctuations of the femtosecond energy transfer times in individual LH2 antenna complexes of purple bacteria. By combining single molecule results with ensemble spectroscopy through a unified theoretical description of both, we show how the protein fluctuations alter the excitation energy transfer dynamics. We find that from the thirteen orders of magnitude of possible timescales from picoseconds to minutes, the relevant fluctuations occur predominantly on a biological timescale of seconds, i.e. in the domain of slow protein motion. The measured spectra and dynamics can be explained by the protein modulating pigment excitation energies only. Moreover, we find that the small spread of pigment mean energies allows for excitation delocalization between the coupled pigments to survive. These unique features provide fast energy transport even in the presence of disorder. We conclude that this is the mechanism that enables LH2 to operate as a robust light-harvester, in spite of its intrinsically noisy biological environment.
[Mh] Termos MeSH primário: Complexos de Proteínas Captadores de Luz/química
[Mh] Termos MeSH secundário: Alphaproteobacteria/metabolismo
Transferência de Energia
Complexos de Proteínas Captadores de Luz/metabolismo
Estrutura Quaternária de Proteína
Teoria Quântica
Espectrometria de Fluorescência
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Light-Harvesting Protein Complexes)
[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:180126
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06139k


  4 / 13049 MEDLINE  
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[PMID]:29352301
[Au] Autor:Shah BS; Ashwood HE; Harrop SJ; Farrugia DN; Paulsen IT; Mabbutt BC
[Ad] Endereço:Department of Molecular Sciences, Macquarie University, Sydney, Australia.
[Ti] Título:Crystal structure of a UDP-GlcNAc epimerase for surface polysaccharide biosynthesis in Acinetobacter baumannii.
[So] Source:PLoS One;13(1):e0191610, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:With new strains of Acinetobacter baumannii undergoing genomic analysis, it has been possible to define regions of genomic plasticity (RGPs), encoding specific adaptive elements. For a selected RGP from a community-derived isolate of A. baumannii, we outline sequences compatible with biosynthetic machinery of surface polysaccharides, specifically enzymes utilized in the dehydration and conversion of UDP-N-acetyl-D-glucosamine (UDP-D-GlcNAc). We have determined the crystal structure of one of these, the epimerase Ab-WbjB. This dehydratase belongs to the 'extended' short-chain dehydrogenase/reductase (SDR) family, related in fold to previously characterised enzymes CapE and FlaA1. Our 2.65Å resolution structure of Ab-WbjB shows a hexamer, organised into a trimer of chain pairs, with coenzyme NADP+ occupying each chain. Specific active-site interactions between each coenzyme and a lysine quaternary group of a neighbouring chain interconnect adjacent dimers, so stabilising the hexameric form. We show UDP-GlcNAc to be a specific substrate for Ab-WbjB, with binding evident by ITC (Ka = 0.23 µmol-1). The sequence of Ab-WbjB shows variation from the consensus active-site motifs of many SDR enzymes, demonstrating a likely catalytic role for a specific threonine sidechain (as an alternative to tyrosine) in the canonical active site chemistry of these epimerases.
[Mh] Termos MeSH primário: Acinetobacter baumannii/enzimologia
Proteínas de Bactérias/química
Carboidratos Epimerases/química
[Mh] Termos MeSH secundário: Acinetobacter baumannii/genética
Acinetobacter baumannii/isolamento & purificação
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Carboidratos Epimerases/genética
Carboidratos Epimerases/metabolismo
Domínio Catalítico
Cristalografia por Raios X
Seres Humanos
Modelos Moleculares
Polissacarídeos Bacterianos/biossíntese
Conformação Proteica
Domínios Proteicos
Estrutura Quaternária de Proteína
Homologia de Sequência de Aminoácidos
Eletricidade Estática
Homologia Estrutural de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Polysaccharides, Bacterial); EC 5.1.3.- (Carbohydrate Epimerases)
[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:180121
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191610


  5 / 13049 MEDLINE  
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[PMID]:29260810
[Au] Autor:Chang S; Mizuno M; Ishikawa H; Mizutani Y
[Ad] Endereço:Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan. mztn@chem.sci.osaka-u.ac.jp.
[Ti] Título:Tertiary dynamics of human adult hemoglobin fixed in R and T quaternary structures.
[So] Source:Phys Chem Chem Phys;20(5):3363-3372, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein dynamics of human adult hemoglobin and its mutants restricted in R and T quaternary states following ligand photolysis were studied by time-resolved resonance Raman spectroscopy. In the time-resolved spectra, we observed spectral changes of in-plane stretching modes of heme and the iron-histidine stretching mode of the Fe-His bond for all the hemoglobin samples. The ßD99N mutant, which adopts the R state in both the ligand-bound and the deoxy forms, showed similar temporal behaviors in time-resolved resonance Raman spectra as wild-type recombinant hemoglobin until 10 µs, consistent with the fact that the mutant undergoes only the tertiary structural changes in the R state. The ßN102T mutant, which adopts the T state in both the ligand-bound and the deoxy forms, showed much slower tertiary structural changes, suggesting that the EF helical motion is decelerated by the change of the intersubunit interactions. The present data indicate that the allosteric kinetic response between the interhelical hydrogen bonds of the EF helices and the intersubunit hydrogen bonds is bidirectional. The implications of these results for understanding the allosteric pathway of Hb are discussed in detail.
[Mh] Termos MeSH primário: Hemoglobinas/química
[Mh] Termos MeSH secundário: Adulto
Heme/química
Heme/metabolismo
Hemoglobinas/genética
Hemoglobinas/metabolismo
Histidina/química
Histidina/metabolismo
Seres Humanos
Ligações de Hidrogênio
Mutagênese Sítio-Dirigida
Estrutura Quaternária de Proteína
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 0 (Recombinant Proteins); 42VZT0U6YR (Heme); 4QD397987E (Histidine)
[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:171221
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06287g


  6 / 13049 MEDLINE  
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[PMID]:29351320
[Au] Autor:Kumar P; van Son M; Zheng T; Valdink D; Raap J; Kros A; Huber M
[Ad] Endereço:Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands.
[Ti] Título:Coiled-coil formation of the membrane-fusion K/E peptides viewed by electron paramagnetic resonance.
[So] Source:PLoS One;13(1):e0191197, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The interaction of the complementary K (Ac-(KIAALKE)3-GW-NH2) and E (Ac-(EIAALEK)3-GY-NH2) peptides, components of the zipper of an artificial membrane fusion system (Robson Marsden H. et al. Angew Chemie Int Ed. 2009) is investigated by electron paramagnetic resonance (EPR). By frozen solution continuous-wave EPR and double electron-electron resonance (DEER), the distance between spin labels attached to the K- and to the E-peptide is measured. Three constructs of spin-labelled K- and E-peptides are used in five combinations for low temperature investigations. The K/E heterodimers are found to be parallel, in agreement with previous studies. Also, K homodimers in parallel orientation were observed, a finding that was not reported before. Comparison to room-temperature, solution EPR shows that the latter method is less specific to detect this peptide-peptide interaction. Combining frozen solution cw-EPR for short distances (1.8 nm to 2.0 nm) and DEER for longer distances thus proves versatile to detect the zipper interaction in membrane fusion. As the methodology can be applied to membrane samples, the approach presented suggests itself for in-situ studies of the complete membrane fusion process, opening up new avenues for the study of membrane fusion.
[Mh] Termos MeSH primário: Proteínas de Fusão de Membrana/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Simulação por Computador
Espectroscopia de Ressonância de Spin Eletrônica
Fusão de Membrana/fisiologia
Proteínas de Fusão de Membrana/fisiologia
Modelos Moleculares
Oligopeptídeos/química
Domínios e Motivos de Interação entre Proteínas
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Marcadores de Spin
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Fusion Proteins); 0 (Oligopeptides); 0 (Spin Labels)
[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:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191197


  7 / 13049 MEDLINE  
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[PMID]:29198706
[Au] Autor:Kim S; Kim KJ
[Ad] Endereço:School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu, 41566, Republic of Korea; KNU Institute for Microorganisms, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu, 41566, Republic of Korea.
[Ti] Título:Structural insight into the substrate specificity of acyl-CoA oxidase1 from Yarrowia lipolytica for short-chain dicarboxylyl-CoAs.
[So] Source:Biochem Biophys Res Commun;495(2):1628-1634, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyl-CoA oxidase (ACOX) plays an important role in fatty acid degradation. The enzyme catalyzes the first reaction in peroxisomal fatty acid ß-oxidation by reducing acyl-CoA to 2-trans-enoyl-CoA. The yeast Yarrowia lipolytica is able to utilize fatty acids, fats, and oil as carbon sources to produce valuable bioproducts. We determined the crystal structure of ACOX1 from Y. lipolytica (YlACOX1) at a resolution of 2.5 Å. YlACOX1 forms a homodimer, and the monomeric structure is composed of four domains, the Nα, Nß, Cα1, and Cα2. The FAD cofactor is bound at the dimerization interface between the Nß- and Cα1-domains. The substrate-binding tunnel formed by the interface between the Nα-, Nß-, and Cα1-domains is located proximal to FAD. Amino acid and structural comparisons of YlACOX1 with other ACOXs show that the substrate-binding pocket of YlACOX1 is much smaller than that of the medium- or long-chain ACOXs but is rather similar to that of the short-chain ACOXs. Moreover, the hydrophilicity of residues constituting the end region of the substrate-binding pocket in YlACOX1 is quite similar to those in the short-chain ACOXs but different from those of the medium- or long-chain ACOXs. These observations provide structural insights how YlACOX1 prefers short-chain dicarboxylyl-CoAs as a substrate.
[Mh] Termos MeSH primário: Acil-CoA Oxidase/química
Acil-CoA Oxidase/metabolismo
Proteínas Fúngicas/química
Proteínas Fúngicas/metabolismo
Yarrowia/enzimologia
[Mh] Termos MeSH secundário: Acil Coenzima A/química
Acil Coenzima A/metabolismo
Acil-CoA Oxidase/genética
Sequência de Aminoácidos
Domínio Catalítico
Cristalografia por Raios X
Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas Fúngicas/genética
Interações Hidrofóbicas e Hidrofílicas
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Modelos Moleculares
Estrutura Quaternária de Proteína
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Yarrowia/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Fungal Proteins); 0 (Isoenzymes); 146-14-5 (Flavin-Adenine Dinucleotide); EC 1.3.3.6 (Acyl-CoA Oxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  8 / 13049 MEDLINE  
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[PMID]:29197577
[Au] Autor:Liew CW; Hynson RM; Ganuelas LA; Shah-Mohammadi N; Duff AP; Kojima S; Homma M; Lee LK
[Ad] Endereço:School of Medical Sciences, The University of New South Wales, Australia.
[Ti] Título:Solution structure analysis of the periplasmic region of bacterial flagellar motor stators by small angle X-ray scattering.
[So] Source:Biochem Biophys Res Commun;495(2):1614-1619, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bacterial flagellar motor drives the rotation of helical flagellar filaments to propel bacteria through viscous media. It consists of a dynamic population of mechanosensitive stators that are embedded in the inner membrane and activate in response to external load. This entails assembly around the rotor, anchoring to the peptidoglycan layer to counteract torque from the rotor and opening of a cation channel to facilitate an influx of cations, which is converted into mechanical rotation. Stator complexes are comprised of four copies of an integral membrane A subunit and two copies of a B subunit. Each B subunit includes a C-terminal OmpA-like peptidoglycan-binding (PGB) domain. This is thought to be linked to a single N-terminal transmembrane helix by a long unstructured peptide, which allows the PGB domain to bind to the peptidoglycan layer during stator anchoring. The high-resolution crystal structures of flagellar motor PGB domains from Salmonella enterica (MotB ) and Vibrio alginolyticus (PomB ) have previously been elucidated. Here, we use small-angle X-ray scattering (SAXS). We show that unlike MotB , the dimeric conformation of the PomB in solution differs to its crystal structure, and explore the functional relevance by characterising gain-of-function mutants as well as wild-type constructs of various lengths. These provide new insight into the conformational diversity of flagellar motor PGB domains and experimental verification of their overall topology.
[Mh] Termos MeSH primário: Proteínas da Membrana Bacteriana Externa/química
Proteínas de Bactérias/química
Flagelos/química
Proteínas Motores Moleculares/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas da Membrana Bacteriana Externa/genética
Proteínas de Bactérias/genética
Modelos Moleculares
Proteínas Motores Moleculares/genética
Domínios Proteicos
Estrutura Quaternária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Salmonella enterica/química
Salmonella enterica/genética
Espalhamento a Baixo Ângulo
Homologia de Sequência de Aminoácidos
Soluções
Vibrio alginolyticus/química
Vibrio alginolyticus/genética
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (Molecular Motor Proteins); 0 (MotB protein, Bacteria); 0 (PomB protein, bacteria); 0 (Recombinant Proteins); 0 (Solutions)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171204
[St] Status:MEDLINE


  9 / 13049 MEDLINE  
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[PMID]:28741756
[Au] Autor:Järvå M; Lay FT; Hulett MD; Kvansakul M
[Ad] Endereço:Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Vic, Australia.
[Ti] Título:Structure of the defensin NsD7 in complex with PIP reveals that defensin : lipid oligomer topologies are dependent on lipid type.
[So] Source:FEBS Lett;591(16):2482-2490, 2017 08.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Defensins are innate immune molecules that upon recognition of specific phospholipids can disrupt microbial membranes by forming oligomeric assemblies. Structures of two related plant defensins, NaD1 and NsD7, bound to phosphatidylinositol 4,5-bisphosphate (PIP ) and phosphatidic acid (PA), respectively, revealed striking differences in their oligomeric topologies. To understand how NsD7 binds different phospholipids and rationalize the different topologies, we determined the structure of an NsD7-PIP complex. This structure reveals fundamental differences in phospholipid binding compared to NsD7-PA, and an oligomeric topology nearly identical to the previously determined NaD1-PIP complex, establishing that the PIP fibril topology is conserved between NaD1 and NsD7. Our findings highlight the remarkable ability of defensins to bind different types of phospholipids to form oligomeric fibrils with diverse topologies.
[Mh] Termos MeSH primário: Defensinas/química
Defensinas/metabolismo
Fosfatos de Fosfatidilinositol/química
Fosfatos de Fosfatidilinositol/metabolismo
Multimerização Proteica
[Mh] Termos MeSH secundário: Membrana Celular/metabolismo
Seres Humanos
Modelos Moleculares
Ácidos Fosfatídicos/metabolismo
Ligação Proteica
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Defensins); 0 (Phosphatidic Acids); 0 (Phosphatidylinositol Phosphates); 0 (phosphatidylinositol 3,4-diphosphate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12761


  10 / 13049 MEDLINE  
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[PMID]:29348579
[Au] Autor:Lin Z; Liu J; Ding H; Xu F; Liu H
[Ad] Endereço:State Key Laboratory of Natural and Biomimetic Drugs & Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing, 100191, China.
[Ti] Título:Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation.
[So] Source:Nat Commun;9(1):268, 2018 01 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:SALM5, a synaptic adhesion molecule implicated in autism, induces presynaptic differentiation through binding to the LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) that have been highlighted as presynaptic hubs for synapse formation. The mechanisms underlying SALM5/LAR-RPTP interaction remain unsolved. Here we report crystal structures of human SALM5 LRR-Ig alone and in complex with human PTPδ Ig1-3 (MeA ). Distinct from other LAR-RPTP ligands, SALM5 mainly exists as a dimer with LRR domains from two protomers packed in an antiparallel fashion. In the 2:2 heterotetrameric SALM5/PTPδ complex, a SALM5 dimer bridges two separate PTPδ molecules. Structure-guided mutations and heterologous synapse formation assays demonstrate that dimerization of SALM5 is prerequisite for its functionality in inducing synaptic differentiation. This study presents a structural template for the SALM family and reveals a mechanism for how a synaptic adhesion molecule directly induces cis-dimerization of LAR-RPTPs into higher-order signaling assembly.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular Neuronais/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
[Mh] Termos MeSH secundário: Baculoviridae
Dimerização
Células HEK293
Seres Humanos
Domínios de Imunoglobulina
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (SALM5 protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02414-2



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