Ke. Prehoda et al., Structure of the enabled VASP homology 1 domain-peptide complex: A key component in the spatial control of actin assembly, CELL, 97(4), 1999, pp. 471-480
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 f
or targeting the actin assembly machinery to sites of cytoskeletal remodeli
ng. The crystal structure of the mammalian Enabled (Mena) EVH1 domain compl
exed with a peptide ligand reveals a mechanism of recognition distinct from
that used by other proline-binding modules. The EVH1 domain fold is unexpe
ctedly similar to that of the pleckstrin homology domain, a membrane locali
zation module. This finding demonstrates the functional plasticity of the p
leckstrin homology fold as a binding scaffold and suggests that membrane as
sociation may play an auxiliary role in EVH1 targeting.