3ixe

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Revision as of 09:33, 27 March 2013

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Template:STRUCTURE 3ixe

Contents 1 Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase 2 Function 3 About this Structure 4 Reference

Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase

Template:ABSTRACT PUBMED 19963065

Function

[ILK_HUMAN] Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B. [LIMS2_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. Plays a role in modulating cell spreading and migration.^[1]

About this Structure

3ixe is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

• Chiswell BP, Stiegler AL, Razinia Z, Nalibotski E, Boggon TJ, Calderwood DA. Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase. J Struct Biol. 2010 Apr;170(1):157-63. Epub 2009 Dec 4. PMID:19963065 doi:10.1016/j.jsb.2009.12.002

1. ↑ Zhang Y, Chen K, Guo L, Wu C. Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration. J Biol Chem. 2002 Oct 11;277(41):38328-38. Epub 2002 Aug 6. PMID:12167643 doi:10.1074/jbc.M205576200