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

A. A. Fedorov, E. Fedorov, F. Gertler, Steven C. Almo

Research output: Contribution to journalArticle

93 Citations (Scopus)

Abstract

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

Original languageEnglish (US)
Pages (from-to)661-665
Number of pages5
JournalNature Structural Biology
Volume6
Issue number7
DOIs
StatePublished - 1999

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Proline
Ligands
Phosphotyrosine
src Homology Domains
Actins
Proteins
Peptides
platelet protein P47
Protein Domains

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. / Fedorov, A. A.; Fedorov, E.; Gertler, F.; Almo, Steven C.

In: Nature Structural Biology, Vol. 6, No. 7, 1999, p. 661-665.

Research output: Contribution to journalArticle

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