1evh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1evh |SIZE=350|CAPTION= <scene name='initialview01'>1evh</scene>, resolution 1.8Å | |PDB= 1evh |SIZE=350|CAPTION= <scene name='initialview01'>1evh</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1evh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1evh OCA], [http://www.ebi.ac.uk/pdbsum/1evh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1evh RCSB]</span> | |||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Lim, W A.]] | [[Category: Lim, W A.]] | ||
[[Category: Prehoda, K E.]] | [[Category: Prehoda, K E.]] | ||
[[Category: actin dynamic]] | [[Category: actin dynamic]] | ||
[[Category: molecular recognition]] | [[Category: molecular recognition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:10:22 2008'' | ||
Revision as of 17:10, 30 March 2008
| |||||||||||||
| 1evh, resolution 1.8Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | ACE | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE
Overview
The Enabled/VASP homology 1 (EVH1; also called WH1) domain is an interaction module found in several proteins implicated in actin-based cell motility. EVH1 domains bind the consensus proline-rich motif FPPPP and are required for targeting the actin assembly machinery to sites of cytoskeletal remodeling. The crystal structure of the mammalian Enabled (Mena) EVH1 domain complexed with a peptide ligand reveals a mechanism of recognition distinct from that used by other proline-binding modules. The EVH1 domain fold is unexpectedly similar to that of the pleckstrin homology domain, a membrane localization module. This finding demonstrates the functional plasticity of the pleckstrin homology fold as a binding scaffold and suggests that membrane association may play an auxiliary role in EVH1 targeting.
About this Structure
1EVH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly., Prehoda KE, Lee DJ, Lim WA, Cell. 1999 May 14;97(4):471-80. PMID:10338211
Page seeded by OCA on Sun Mar 30 20:10:22 2008
