1evh: Difference between revisions
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[[Image:1evh.jpg|left|200px]] | [[Image:1evh.jpg|left|200px]] | ||
'''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE''' | {{Structure | ||
|PDB= 1evh |SIZE=350|CAPTION= <scene name='initialview01'>1evh</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EVH is a [ | 1EVH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EVH OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10338211 10338211] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Prehoda, K E.]] | [[Category: Prehoda, K E.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: actin | [[Category: actin dynamic]] | ||
[[Category: molecular recognition]] | [[Category: molecular recognition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:49 2008'' | ||
Revision as of 09:00, 20 March 2008
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| 1evh, resolution 1.8Å | |||||||||||||
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| Ligands: | ACE | ||||||||||||
| 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
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