1evh: Difference between revisions

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[[Image:1evh.jpg|left|200px]]
[[Image:1evh.jpg|left|200px]]


{{Structure
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|DOMAIN=
{{STRUCTURE_1evh| PDB=1evh  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1evh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1evh OCA], [http://www.ebi.ac.uk/pdbsum/1evh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1evh RCSB]</span>
}}


'''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE'''
'''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE'''
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[[Category: Lim, W A.]]
[[Category: Lim, W A.]]
[[Category: Prehoda, K E.]]
[[Category: Prehoda, K E.]]
[[Category: actin dynamic]]
[[Category: Actin dynamic]]
[[Category: molecular recognition]]
[[Category: Molecular recognition]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:10:22 2008''

Revision as of 12:33, 2 May 2008

File:1evh.jpg

Template:STRUCTURE 1evh

EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE


Overview

The Enabled/VASP homology 1 (EVH1; also called WH1) domain is an interaction module found in several proteins implicated in actin-based cell motility. EVH1 domains bind the consensus proline-rich motif FPPPP and are required for targeting the actin assembly machinery to sites of cytoskeletal remodeling. The crystal structure of the mammalian Enabled (Mena) EVH1 domain complexed with a peptide ligand reveals a mechanism of recognition distinct from that used by other proline-binding modules. The EVH1 domain fold is unexpectedly similar to that of the pleckstrin homology domain, a membrane localization module. This finding demonstrates the functional plasticity of the pleckstrin homology fold as a binding scaffold and suggests that membrane association may play an auxiliary role in EVH1 targeting.

About this Structure

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

Reference

Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly., Prehoda KE, Lee DJ, Lim WA, Cell. 1999 May 14;97(4):471-80. PMID:10338211 Page seeded by OCA on Fri May 2 15:33:56 2008

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