6u4m: Difference between revisions

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'''Unreleased structure'''


The entry 6u4m is ON HOLD  until Paper Publication
==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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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]]
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