1EVH

EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE

Summary for 1EVH

• Entry DOI: 10.2210/pdb1evh/pdb
• Descriptor: PROTEIN (MENA EVH1 DOMAIN), Peptide ACTA (3 entities in total)
• Functional Keywords: molecular recognition, actin dynamics, contractile protein
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 13279.04

Authors

Prehoda, K.E.,Lee, D.J.,Lim, W.A. (deposition date: 1999-04-21, release date: 1999-05-21, Last modification date: 2024-11-13)

Primary citation

Prehoda, K.E.,Lee, D.J.,Lim, W.A.
Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly.
Cell(Cambridge,Mass.), 97:471-480, 1999

PubMed Abstract: 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.

PubMed: 10338211
DOI: 10.1016/S0092-8674(00)80757-6

Experimental method

X-RAY DIFFRACTION (1.8 Å)