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6fmm
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human full-length vinculin-T12-A974K (residues 1-1066)== | |
| + | <StructureSection load='6fmm' size='340' side='right' caption='[[6fmm]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6fmm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FMM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FMM FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fmm OCA], [http://pdbe.org/6fmm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fmm RCSB], [http://www.ebi.ac.uk/pdbsum/6fmm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fmm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Defects in VCL are the cause of cardiomyopathy dilated type 1W (CMD1W) [MIM:[http://omim.org/entry/611407 611407]]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:11815424</ref> <ref>PMID:16236538</ref> Defects in VCL are the cause of familial hypertrophic cardiomyopathy type 15 (CMH15) [MIM:[http://omim.org/entry/613255 613255]]. It is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:16712796</ref> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/VINC_HUMAN VINC_HUMAN]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:20484056</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Focal adhesions (FAs) are multi-protein complexes that connect the actin cytoskeleton to the extracellular matrix, via integrin receptors. The growth, stability and adhesive functionality of these structures are tightly regulated by mechanical stress, yet, despite the extensive characterization of the integrin adhesome, the detailed molecular mechanisms underlying FA mechanosensitivity are still unclear. Besides talin, another key candidate for regulating FA-associated mechanosensing, is vinculin, a prominent FA component, which possesses either closed ("auto-inhibited") or open ("active") conformation. A direct experimental demonstration, however, of the conformational transition between the two states is still absent. In this study, we combined multiple structural and biological approaches to probe the transition from the auto-inhibited to the active conformation, and determine its effects on FA structure and dynamics. We further show that the transition from a closed to an open conformation requires two sequential steps that can differentially regulate FA growth and stability. | ||
| - | + | Conformational states during vinculin unlocking differentially regulate focal adhesion properties.,Chorev DS, Volberg T, Livne A, Eisenstein M, Martins B, Kam Z, Jockusch BM, Medalia O, Sharon M, Geiger B Sci Rep. 2018 Feb 9;8(1):2693. doi: 10.1038/s41598-018-21006-8. PMID:29426917<ref>PMID:29426917</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6fmm" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chorev, D S]] | ||
[[Category: Eisenstein, M]] | [[Category: Eisenstein, M]] | ||
| - | [[Category: Sharon, M]] | ||
| - | [[Category: Kam, Z]] | ||
| - | [[Category: Chorev, D.S]] | ||
| - | [[Category: Martins, B]] | ||
[[Category: Geiger, B]] | [[Category: Geiger, B]] | ||
| + | [[Category: Jockusch, B M]] | ||
| + | [[Category: Kam, Z]] | ||
[[Category: Livne, A]] | [[Category: Livne, A]] | ||
| - | [[Category: | + | [[Category: Martins, B]] |
| + | [[Category: Medalia, O]] | ||
| + | [[Category: Sharon, M]] | ||
[[Category: Volberg, T]] | [[Category: Volberg, T]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Mechanosensitive self-inhibition adapter]] | ||
Revision as of 07:32, 22 February 2018
Crystal structure of human full-length vinculin-T12-A974K (residues 1-1066)
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