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1qc6

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(New page: 200px<br /><applet load="1qc6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qc6, resolution 2.6&Aring;" /> '''EVH1 domain from ENA/...)
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Revision as of 22:26, 20 November 2007


1qc6, resolution 2.6Å

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EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide

Overview

The Ena-VASP homology (EVH1) domain is a protein interaction module found, in several proteins that are involved in transducing migratory and, morphological signals into cytoskeletal reorganization. EVH1 specifically, recognizes proline-rich sequences in its binding partners and directs the, localization and formation of multicomponent assemblies involved in, actin-based motile processes and neural development. The structure of the, complex between an EVH1 domain and the target peptide sequence EFPPPPT, identifies the interactions responsible for recognition and distinguishes, it from other proline-rich binding modules, including SH3 and WW domains., Surprisingly, the EVH1 domain has structural similarity to pleckstrin, homology (PH), phosphotyrosine-binding (PTB) and ran-binding (RanBD), domains.

About this Structure

1QC6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function., Fedorov AA, Fedorov E, Gertler F, Almo SC, Nat Struct Biol. 1999 Jul;6(7):661-5. PMID:10404224

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