1QC6

EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide

Summary for 1QC6

• Entry DOI: 10.2210/pdb1qc6/pdb
• Descriptor: EVH1 DOMAIN FROM ENA/VASP-LIKE PROTEIN, PHE-GLU-PHE-PRO-PRO-PRO-PRO-THR-ASP-GLU-GLU (3 entities in total)
• Functional Keywords: an incomplete seven stranded anti-parallel beta barrel closed by an alpha helix, evh1 domain, actin-based cell motility, interaction module, structural protein
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cytoplasm, cytoskeleton : P70429
• Total number of polymer chains: 4
• Total formula weight: 32202.64

Authors

Fedorov, A.A.,Fedorov, E.V.,Gertler, F.B.,Almo, S.C. (deposition date: 1999-05-17, release date: 1999-05-25, Last modification date: 2024-11-20)

Primary citation

Fedorov, A.A.,Fedorov, E.,Gertler, F.,Almo, S.C.
Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function
Nat.Struct.Biol., 6:661-665, 1999

PubMed 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.

PubMed: 10404224
DOI: 10.1038/10717

Experimental method

X-RAY DIFFRACTION (2.6 Å)