Work

Structure of EVH1: a Novel Proline-Rich Ligand Binding Module Involved in Cytoskeletal Dynamics and Neural Function

Year: 2000

Type: article

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.

Source: Acta Crystallographica Section A Foundations of Crystallography

DOI: 10.1107/s0108767300026210

Authors: A. A. Fedorov, E. Fedorov, F. Gertler, S. C. Almo

Institutions: Albert Einstein College of Medicine, University of Würzburg, Center for Cancer Research, Massachusetts Institute of Technology

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W1979468989

FWCI: 0.12

Cites:

Cited by: 3

Related to: 10