Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. |
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| Authors: | K E Prehoda D J Lee W A Lim |
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| Institution: | Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA. |
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| 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. |
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