1qc6
From Proteopedia
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'''EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide''' | '''EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide''' | ||
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[[Category: Fedorov, E V.]] | [[Category: Fedorov, E V.]] | ||
[[Category: Gertler, F B.]] | [[Category: Gertler, F B.]] | ||
| - | [[Category: | + | [[Category: Actin-based cell motility]] |
| - | [[Category: | + | [[Category: An incomplete seven stranded anti-parallel beta barrel closed by an alpha helix]] |
| - | [[Category: | + | [[Category: Evh1 domain]] |
| - | [[Category: | + | [[Category: Interaction module]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:07:07 2008'' | |
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Revision as of 03:07, 3 May 2008
EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide
Overview
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.
About this Structure
1QC6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function., Fedorov AA, Fedorov E, Gertler F, Almo SC, Nat Struct Biol. 1999 Jul;6(7):661-5. PMID:10404224 Page seeded by OCA on Sat May 3 06:07:07 2008
