2cia

From Proteopedia

Revision as of 12:05, 30 October 2007

HUMAN NCK2 SH2-DOMAIN IN COMPLEX WITH A DECAPHOSPHOPEPTIDE FROM TRANSLOCATED INTIMIN RECEPTOR (TIR) OF EPEC

Overview

Nck proteins are essential Src homology (SH) 2 and SH3 domain-bearing, adapters that modulate actin cytoskeleton dynamics by linking proline-rich, effector molecules to tyrosine kinases or phosphorylated signaling, intermediates. Two mammalian pathogens, enteropathogenic Escherichia coli, and vaccinia virus, exploit Nck as part of their infection strategy., Conflicting data indicate potential differences in the recognition, specificities of the SH2 domains of the isoproteins Nck1 (Nckalpha) and, Nck2 (Nckbeta and Grb4). We have characterized the binding specificities, of both SH2 domains and find them to be essentially indistinguishable., Crystal structures of both domains in complex with phosphopeptides derived, from the enteropathogenic E. coli protein Tir concur in identifying highly, ... [(full description)]

About this Structure

2CIA is a [Protein complex] structure of sequences from [Homo sapiens] with ACE, MPD and IPA as [ligands]. Structure known Active Site: AC2. Full crystallographic information is available from [OCA].

Reference

The phosphotyrosine peptide binding specificity of Nck1 and Nck2 Src homology 2 domains., Frese S, Schubert WD, Findeis AC, Marquardt T, Roske YS, Stradal TE, Heinz DW, J Biol Chem. 2006 Jun 30;281(26):18236-45. Epub 2006 Apr 24. PMID:16636066

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