1u5s

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Revision as of 17:25, 12 November 2007

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NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain

Overview

Weak protein-protein interactions (PPIs) (K(D) > 10(-6) M) are critical, determinants of many biological processes. However, in contrast to a large, growing number of well-characterized, strong PPIs, the weak PPIs, especially those with K(D) > 10(-4) M, are poorly explored. Genome wide, there exist few 3D structures of weak PPIs with K(D) > 10(-4) M, and none, with K(D) > 10(-3) M. Here, we report the NMR structure of an extremely, weak focal adhesion complex (K(D) approximately 3 x 10(-3) M) between, Nck-2 SH3 domain and PINCH-1 LIM4 domain. The structure exhibits a, remarkably small and polar interface with distinct binding modes for both, SH3 and LIM domains. Such an interface suggests a transient Nck-2/PINCH-1, association process that may trigger rapid focal adhesion turnover during, integrin signaling. Genetic rescue experiments demonstrate that this, interface is indeed involved in mediating cell shape change and migration., Together, the data provide a molecular basis for an ultraweak PPI in, regulating focal adhesion dynamics during integrin signaling.

About this Structure

1U5S is a Protein complex structure of sequences from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility., Vaynberg J, Fukuda T, Chen K, Vinogradova O, Velyvis A, Tu Y, Ng L, Wu C, Qin J, Mol Cell. 2005 Feb 18;17(4):513-23. PMID:15721255

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