Base de dados : MEDLINE
Pesquisa : G02.206 [Categoria DeCS]
Referências encontradas : 28960 [refinar]
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  1 / 28960 MEDLINE  
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[PMID]:28471385
[Au] Autor:Sun K; Tao ML; Tu YB; Wang JZ
[Ad] Endereço:School of Physical Science and Technology, MOE Key Laboratory on Luminescence and Real-Time Analysis, Southwest University, Chongqing 400715, China. sun.andkai@163.com.
[Ti] Título:Off-Center Rotation of CuPc Molecular Rotor on a Bi(111) Surface and the Chiral Feature.
[So] Source:Molecules;22(5), 2017 May 04.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Molecular rotors with an off-center axis and the chiral feature of achiral CuPc molecules on a semi-metallic Bi(111) surface have been investigated by means of a scanning tunneling microscopy (STM) at liquid nitrogen (LN2) temperature. The rotation axis of each CuPc molecular rotor is located at the end of a phthalocyanine group. As molecular coverage increases, the CuPc molecules are self-assembled into various nanoclusters and finally into two-dimensional (2D) domains, in which each CuPc molecule exhibits an apparent chiral feature. Such chiral features of the CuPc molecules can be attributed to the combined effect of asymmetric charge transfer between the CuPc and Bi(111) substrate, and the intermolecular van der Waals interactions.
[Mh] Termos MeSH primário: Bismuto/química
[Mh] Termos MeSH secundário: Dimerização
Microscopia de Tunelamento
Estereoisomerismo
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
U015TT5I8H (Bismuth)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  2 / 28960 MEDLINE  
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[PMID]:29353723
[Au] Autor:Wu YZ; Zhang HW; Sun ZH; Dai JG; Hu YC; Li R; Lin PC; Xia GY; Wang LY; Qiu BL; Zhang JF; Ge GB; Lin S
[Ad] Endereço:State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China.
[Ti] Título:Bysspectin A, an unusual octaketide dimer and the precursor derivatives from the endophytic fungus Byssochlamys spectabilis IMM0002 and their biological activities.
[So] Source:Eur J Med Chem;145:717-725, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Bysspectin A (1), a polyketide-derived octaketide dimer with a novel carbon skeleton, and two new precursor derivatives, bysspectins B and C (2 and 3), were obtained from an organic extract of the endophytic fungus Byssochlamys spectabilis that had been isolated from a leaf tissue of the traditional Chinese medicinal plant Edgeworthia chrysantha, together with a known octaketide, paecilocin A (4). Their structures were determined by HRMS, 1D and 2D NMR spectroscopic analysis. A plausible route for their biosynthetic pathway is proposed. Compounds 1-3 were tested for their antimicrobial activities. Only compound 3 was weakly active against Escherichia coli and Staphyloccocus aureus with MIC values of 32 and 64 µg/mL, respectively. Further, the inhibitory effects on human carboxylesterases (hCE1, hCE2) of compounds 1 and 4 were evaluated. The results demonstrated that bysspectin A (1) was a novel and highly selective inhibitor against hCE2 with the IC value of 2.01 µM. Docking simulation also demonstrated that active compound 1 created interaction with the Ser-288 (the catalytic amino-acid in the catalytic cavity) of hCE2 via hydrogen bonding, revealing its highly selective inhibition toward hCE2.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Byssochlamys/química
Carboxilesterase/antagonistas & inibidores
Hidrolases de Éster Carboxílico/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Escherichia coli/efeitos dos fármacos
Policetídeos/farmacologia
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Antibacterianos/química
Antibacterianos/isolamento & purificação
Biocatálise
Carboxilesterase/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Dimerização
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/química
Inibidores Enzimáticos/isolamento & purificação
Seres Humanos
Testes de Sensibilidade Microbiana
Simulação de Acoplamento Molecular
Estrutura Molecular
Policetídeos/química
Policetídeos/isolamento & purificação
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Enzyme Inhibitors); 0 (Polyketides); 0 (bysspectin A); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.1 (CES1 protein, human); EC 3.1.1.1 (CES2 protein, human); EC 3.1.1.1 (Carboxylesterase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180123
[St] Status:MEDLINE


  3 / 28960 MEDLINE  
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[PMID]:29190078
[Au] Autor:Gonzalez P; Vileno B; Bossak K; El Khoury Y; Hellwig P; Bal W; Hureau C; Faller P
[Ad] Endereço:Institut de Chimie, UMR 7177, CNRS, Université de Strasbourg , 4 rue Blaise Pascal 67000, Strasbourg, France.
[Ti] Título:Cu(II) Binding to the Peptide Ala-His-His, a Chimera of the Canonical Cu(II)-Binding Motifs Xxx-His and Xxx-Zzz-His.
[So] Source:Inorg Chem;56(24):14870-14879, 2017 Dec 18.
[Is] ISSN:1520-510X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peptides and proteins with the N-terminal motifs NH -Xxx-His and NH -Xxx-Zzz-His form well-established Cu(II) complexes. The canonical peptides are Gly-His-Lys and Asp-Ala-His-Lys (from the wound healing factor and human serum albumin, respectively). Cu(II) is bound to NH -Xxx-His via three nitrogens from the peptide and an external ligand in the equatorial plane (called 3N form here). In contrast, Cu(II) is bound to NH -Xxx-Zzz-His via four nitrogens from the peptide in the equatorial plane (called 4N form here). These two motifs are not mutually exclusive, as the peptides with the sequence NH -Xxx-His-His contain both of them. However, this chimera has never been fully explored. In this work, we use a multispectroscopic approach to analyze the Cu(II) binding to the chimeric peptide Ala-His-His (AHH). AHH is capable of forming the 3N- and 4N-type complexes in a pH dependent manner. The 3N form predominates at pH ∼ 4-6.5 and the 4N form at ∼ pH 6.5-10. NMR experiments showed that at pH 8.5, where Cu(II) is almost exclusively bound in the 4N form, the Cu(II)-exchange between AHH or the amidated AHH-NH is fast, in comparison to the nonchimeric 4N form (AAH). Together, the results show that the chimeric AHH can access both Cu(II) coordination types, that minor changes in the second (or further) coordination sphere can impact considerably the equilibrium between the forms, and that Cu kinetic exchange is fast even when Cu-AHH is mainly in the 4N form.
[Mh] Termos MeSH primário: Complexos de Coordenação/química
Cobre/química
Oligopeptídeos/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Dimerização
Espectroscopia de Ressonância de Spin Eletrônica
Concentração de Íons de Hidrogênio
Cinética
Espectroscopia de Ressonância Magnética
Potenciometria
Conformação Proteica
Proteínas/química
Espectroscopia de Infravermelho com Transformada de Fourier
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ala-His-His); 0 (Coordination Complexes); 0 (Oligopeptides); 0 (Proteins); 789U1901C5 (Copper)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1021/acs.inorgchem.7b01996


  4 / 28960 MEDLINE  
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[PMID]:28641463
[Au] Autor:Du SZ; Kuang F; Liu Y; Chen YG; Zhan R
[Ad] Endereço:a School of Chemistry and Chemical Engineering , Yunnan Normal University , Kunming , China.
[Ti] Título:A new dimeric diarylpropane from Horsfieldia tetratepala.
[So] Source:Nat Prod Res;32(2):162-166, 2018 Jan.
[Is] ISSN:1478-6427
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Five compounds, including a new dimeric diarylpropane, were isolated from the petroleum ether extract of the twigs and leaves of Horsfieldia tetratepala. The structures of these compounds were elucidated by spectroscopic analysis. Moreover, the antiproliferative activities of these compounds were tested on cancer cell lines, but none is active.
[Mh] Termos MeSH primário: Myristicaceae/química
Extratos Vegetais/química
Folhas de Planta/química
[Mh] Termos MeSH secundário: Antineoplásicos/isolamento & purificação
Antineoplásicos/farmacologia
Linhagem Celular Tumoral
Dimerização
Seres Humanos
Estrutura Molecular
Propano
Análise Espectral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Plant Extracts); T75W9911L6 (Propane)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1080/14786419.2017.1342087


  5 / 28960 MEDLINE  
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[PMID]:29360855
[Au] Autor:Carrillo JB; Gomez-Casati DF; Martín M; Busi MV
[Ad] Endereço:Centro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Universidad Nacional de Rosario, Rosario, Santa Fe, Argentina.
[Ti] Título:Identification and analysis of OsttaDSP, a phosphoglucan phosphatase from Ostreococcus tauri.
[So] Source:PLoS One;13(1):e0191621, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ostreococcus tauri, the smallest free-living (non-symbiotic) eukaryote yet described, is a unicellular green alga of the Prasinophyceae family. It has a very simple cellular organization and presents a unique starch granule and chloroplast. However, its starch metabolism exhibits a complexity comparable to higher plants, with multiple enzyme forms for each metabolic reaction. Glucan phosphatases, a family of enzymes functionally conserved in animals and plants, are essential for normal starch or glycogen degradation in plants and mammals, respectively. Despite the importance of O. tauri microalgae in evolution, there is no information available concerning the enzymes involved in reversible phosphorylation of starch. Here, we report the molecular cloning and heterologous expression of the gene coding for a dual specific phosphatase from O. tauri (OsttaDSP), homologous to Arabidopsis thaliana LSF2. The recombinant enzyme was purified to electrophoretic homogeneity to characterize its oligomeric and kinetic properties accurately. OsttaDSP is a homodimer of 54.5 kDa that binds and dephosphorylates amylopectin. Also, we also determined that residue C162 is involved in catalysis and possibly also in structural stability of the enzyme. Our results could contribute to better understand the role of glucan phosphatases in the metabolism of starch in green algae.
[Mh] Termos MeSH primário: Clorófitas/enzimologia
Glucanos/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Clonagem Molecular
Dimerização
Cinética
Monoéster Fosfórico Hidrolases/química
Monoéster Fosfórico Hidrolases/genética
Fosforilação
Conformação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glucans); 0 (Recombinant Proteins); EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
[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:180124
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191621


  6 / 28960 MEDLINE  
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[PMID]:29340383
[Au] Autor:Syryamina VN; De Zotti M; Toniolo C; Formaggio F; Dzuba SA
[Ad] Endereço:Institute of Chemical Kinetics and Combustion, RAS, Novosibirsk 630090, Russian Federation. dzuba@kinetics.nsc.ru.
[Ti] Título:Alamethicin self-assembling in lipid membranes: concentration dependence from pulsed EPR of spin labels.
[So] Source:Phys Chem Chem Phys;20(5):3592-3601, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The antimicrobial action of the peptide antibiotic alamethicin (Alm) is commonly related to peptide self-assembling resulting in the formation of voltage-dependent channels in bacterial membranes, which induces ion permeation. To obtain a deeper insight into the mechanism of channel formation, it is useful to know the dependence of self-assembling on peptide concentration. With this aim, we studied Alm F50/5 spin-labeled analogs in a model 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane, for peptide-to-lipid (P/L) ratios varying between 1/1500 and 1/100. Pulsed electron-electron double resonance (PELDOR) spectroscopy reveals that even at the lowest concentration investigated, the Alm molecules assemble into dimers. Moreover, under these conditions, electron spin echo envelope modulation (ESEEM) spectroscopy of D O-hydrated membranes shows an abrupt change from the in-plane to the trans-membrane orientation of the peptide. Therefore, we hypothesize that dimer formation and peptide reorientation are concurrent processes and represent the initial step of peptide self-assembling. By increasing peptide concentration, higher oligomers are formed. A simple kinetic model of equilibrium among monomers, dimers, and pentamers allows for satisfactorily describing the experimental PELDOR data. The inter-label distances in the oligomers obtained from PELDOR experiments become better resolved with increasing P/L ratio, thus suggesting that the supramolecular organization of the higher-order oligomers becomes more defined.
[Mh] Termos MeSH primário: Alameticina/química
Bicamadas Lipídicas/química
[Mh] Termos MeSH secundário: Alameticina/metabolismo
Sequência de Aminoácidos
Dimerização
Espectroscopia de Ressonância de Spin Eletrônica
Cinética
Bicamadas Lipídicas/metabolismo
Fosfatidilcolinas/química
Marcadores de Spin
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipid Bilayers); 0 (Phosphatidylcholines); 0 (Spin Labels); 059QF0KO0R (Water); 27061-78-5 (Alamethicin); TE895536Y5 (1-palmitoyl-2-oleoylphosphatidylcholine)
[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:180118
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp07298h


  7 / 28960 MEDLINE  
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[PMID]:29367148
[Au] Autor:Ting JJ
[Ad] Endereço:De-Font Research Institute, Taichung 40344, Taiwan, ROC. Electronic address: juhilian@gmail.com.
[Ti] Título:Proposal for verifying dipole properties of light-harvesting antennas.
[So] Source:J Photochem Photobiol B;179:134-138, 2018 Feb.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:For light harvesters with a reaction center complex (LH1-RC complex) of three types, we propose an experiment to verify our analysis based upon antenna theories that automatically include the required structural information. Our analysis conforms to the current understanding of light-harvesting antennas in that we can explain known properties of these complexes. We provide an explanation for the functional roles of the notch at the light harvester, a functional role of the polypeptide called PufX or W at the opening, a functional role of the special pair, a reason that the cross section of the light harvester must not be circular, a reason that the light harvester must not be spherical, reasons for the use of dielectric bacteriochlorophylls instead of conductors to make the light harvester, a mechanism to prevent damage from excess sunlight, an advantage of the dimeric form, and reasons for the modular design of nature. Based upon our analysis we provide a mechanism for dimerization. We predict that the dimeric form of light-harvesting complexes is favored under intense sunlight. We further comment upon the classification of the dimeric or S-shape complexes. The S-shape complexes should not be considered as the third type of light harvester but simply as a composite form.
[Mh] Termos MeSH primário: Complexos de Proteínas Captadores de Luz/metabolismo
Modelos Moleculares
[Mh] Termos MeSH secundário: Bacterioclorofilas/química
Bacterioclorofilas/metabolismo
Dimerização
Complexos de Proteínas Captadores de Luz/química
Luz Solar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacteriochlorophylls); 0 (Light-Harvesting Protein Complexes)
[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:180126
[St] Status:MEDLINE


  8 / 28960 MEDLINE  
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[PMID]:29177319
[Au] Autor:Li ZQ; Liao TC; Dong C; Yang JW; Chen XJ; Liu L; Luo Y; Liang YY; Chen WH; Zhou CQ
[Ad] Endereço:Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou 510515, P. R. China. whchen@smu.edu.cn zcqlg@smu.edu.cn.
[Ti] Título:Specifically targeting mixed-type dimeric G-quadruplexes using berberine dimers.
[So] Source:Org Biomol Chem;15(48):10221-10229, 2017 Dec 13.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Three polyether-tethered berberine dimers (1a-c) were studied for their binding affinity, selectivity and thermal stabilization towards human telomeric dimeric quadruplex DNA (G2T1). Compound 1a with the shortest polyether linker showed the highest affinity (K > 10 M ) and 76-508-fold higher selectivity for mixed-type G2T1 over antiparallel G2T1 and three monomeric G-quadruplexes, which are human telomeric monomeric quadruplex G1, c-kit 1 and c-kit 2. Compound 1a induced the formation of quadruplex structures and showed higher thermal stabilization for mixed-type G2T1 than for anti-parallel G2T1, G1 and ds DNA. Spectroscopic studies suggest that compound 1a could bind to mixed-type G2T1 via end-stacking and external binding modes. These results suggest that the polyether linkers in these compounds play an important role in regulating the binding affinity and selectivity towards mixed-type G2T1 and that compound 1a could target mixed-type G2T1 at other genome regions with antiparallel G2T1 and monomeric G-quadruplexes. These results may provide useful guidance for the rational design of selective multimeric G-quadruplex binders and potential anticancer agents.
[Mh] Termos MeSH primário: Berberina/farmacologia
Quadruplex G/efeitos dos fármacos
[Mh] Termos MeSH secundário: Berberina/síntese química
Berberina/química
Dimerização
Seres Humanos
Estrutura Molecular
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0I8Y3P32UF (Berberine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1039/c7ob02326j


  9 / 28960 MEDLINE  
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[PMID]:29292422
[Au] Autor:Zakeri B; Niebling S; Martinéz AG; Sokkar P; Sanchez-Garcia E; Schmuck C; Schlücker S
[Ad] Endereço:Physical Chemistry, University of Duisburg-Essen, 45141 Essen, Germany. sebastian.schluecker@uni-due.de.
[Ti] Título:Molecular recognition of carboxylates in the protein leucine zipper by a multivalent supramolecular ligand: residue-specific, sensitive and label-free probing by UV resonance Raman spectroscopy.
[So] Source:Phys Chem Chem Phys;20(3):1817-1820, 2018 Jan 17.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ultraviolet resonance Raman (UVRR) spectroscopy is a selective, sensitive and label-free vibrational spectroscopic technique. Here, we demonstrate as proof of concept that UVRR can be used for probing the recognition between a multivalent supramolecular ligand and acidic residues in leucine zipper, an α-helical structural motif of many proteins.
[Mh] Termos MeSH primário: Ligantes
Proteínas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Dimerização
Zíper de Leucina
Simulação de Dinâmica Molecular
Estrutura Secundária de Proteína
Proteínas/metabolismo
Análise Espectral Raman
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ligands); 0 (Proteins)
[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:180103
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp04971d


  10 / 28960 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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