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6u4m
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of paxillin LIM4== | |
| + | <StructureSection load='6u4m' size='340' side='right'caption='[[6u4m]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6u4m]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U4M FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6u4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u4m OCA], [http://pdbe.org/6u4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u4m RCSB], [http://www.ebi.ac.uk/pdbsum/6u4m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u4m ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PAXI_HUMAN PAXI_HUMAN]] Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Activation of cell surface receptor integrin has been extensively studied as the first key step to trigger cell adhesion, but the subsequent events, widely regarded as integrin "outside-in" signaling to form supramolecular complexes (focal adhesions [FAs]) to promote dynamic cell adhesion, remain poorly elucidated. Integrin activator kindlin-2 was recently found to associate with paxillin in nascent FAs, implicating an early yet undefined integrin outside-in signaling event. Here we show structurally that kindlin-2 recognizes paxillin via a distinct interface involving the ubiquitin-like kindlin-2 F0 domain and the paxillin LIM4 domain. The interface is adjacent to the membrane binding site of kindlin-2 F0, suggesting a mechanism for kindlin-2 to recruit paxillin to the membrane-proximal site where FA assembly is initiated. Disruption of the interface impaired the localization of paxillin, causing strong defects in FA assembly and cell migration. These data unveil a structural basis of the kindlin-2/paxillin interaction in controlling dynamic cell adhesion. | ||
| - | + | Structural Basis of Paxillin Recruitment by Kindlin-2 in Regulating Cell Adhesion.,Zhu L, Liu H, Lu F, Yang J, Byzova TV, Qin J Structure. 2019 Sep 30. pii: S0969-2126(19)30312-0. doi:, 10.1016/j.str.2019.09.006. PMID:31590942<ref>PMID:31590942</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6u4m" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Qin, J]] | ||
| + | [[Category: Zhu, L]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Lim domain]] | ||
| + | [[Category: Zinc finger]] | ||
Revision as of 07:05, 23 October 2019
Solution structure of paxillin LIM4
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