View source for 6mif


==Lim5 domain of PINCH1 protein==
<StructureSection load='6mif' size='340' side='right'caption='[[6mif]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mif]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MIF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6mif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mif OCA], [https://pdbe.org/6mif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mif RCSB], [https://www.ebi.ac.uk/pdbsum/6mif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mif ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LIMS1_HUMAN LIMS1_HUMAN] Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dynamic communication between integrin-containing complexes (focal adhesions, FAs) and actin filaments is critical for regulating cell adhesion. Pseudokinase ILK plays a key role in this process but the underlying mechanism remains highly elusive. Here we show that by recruiting FA adaptors PINCH and Parvin into a heterotrimeric complex (IPP), ILK triggers F-actin filament bundling - a process known to generate force/mechanical signal to promote cytoskeleton reassembly and dynamic cell adhesion. Structural, biochemical, and functional analyses revealed that the F-actin bundling is orchestrated by two previously unrecognized WASP-Homology-2 actin binding motifs within IPP, one from PINCH and the other from Parvin. Strikingly, this process is also sensitized to Mg-ATP bound to the pseudoactive site of ILK and its dysregulation severely impairs stress fibers formation, cell spreading, and migration. These data identify a crucial mechanism for ILK, highlighting its uniqueness as a pseudokinase to transduce non-catalytic signal and regulate cell adhesion.

Non-catalytic signaling by pseudokinase ILK for regulating cell adhesion.,Vaynberg J, Fukuda K, Lu F, Bialkowska K, Chen Y, Plow EF, Qin J Nat Commun. 2018 Oct 26;9(1):4465. doi: 10.1038/s41467-018-06906-7. PMID:30367047<ref>PMID:30367047</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6mif" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Qin J]]
[[Category: Vaynberg J]]