Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function

The Ena-VASP homology (EVH1) domain is a protein interaction module found i n several proteins that are involved in transducing migratory and morpholog ical signals into cytoskeletal reorganization. EVH1 specifically recognizes proline-rich sequences in its binding partners and directs the localizatio n 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 interact ions responsible for recognition and distinguishes it from other proline-ri ch binding modules, including SH3 and WW domains. Surprisingly, the EVH1 do main has structural similarity to pleckstrin homology (PH), phosphotyrosine -binding (PTB) and ran-binding (RanBD) domains.