1g47

From Proteopedia

Revision as of 13:50, 15 February 2008

1ST LIM DOMAIN OF PINCH PROTEIN

Overview

PINCH is a recently identified adaptor protein that comprises an array of, five LIM domains. PINCH functions through LIM-mediated protein-protein, interactions that are involved in cell adhesion, growth, and, differentiation. The LIM1 domain of PINCH interacts with integrin-linked, kinase (ILK), thereby mediating focal adhesions via a specific, integrin/ILK signaling pathway. We have solved the NMR structure of the, PINCH LIM1 domain and characterized its binding to ILK. LIM1 contains two, contiguous zinc fingers of the CCHC and CCCH types and adopts a global, fold similar to that of functionally distinct LIM domains from, cysteine-rich protein and cysteine-rich intestinal protein families with, CCHC and CCCC zinc finger types. Gel-filtration and NMR experiments, demonstrated a 1:1 complex between PINCH LIM1 and the ankyrin repeat, domain of ILK. A chemical shift mapping experiment identified regions in, PINCH LIM1 that are important for interaction with ILK. Comparison of, surface features between PINCH LIM1 and other functionally different LIM, domains indicated that the LIM motif might have a highly variable mode in, recognizing various target proteins.

About this Structure

1G47 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain., Velyvis A, Yang Y, Wu C, Qin J, J Biol Chem. 2001 Feb 16;276(7):4932-9. Epub 2000 Nov 14. PMID:11078733

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