1evh

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[[Image:1evh.jpg|left|200px]]<br /><applet load="1evh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1evh.jpg|left|200px]]
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caption="1evh, resolution 1.8&Aring;" />
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'''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE'''<br />
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{{Structure
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|PDB= 1evh |SIZE=350|CAPTION= <scene name='initialview01'>1evh</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1EVH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EVH OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10338211 10338211]
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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]]
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[[Category: actin dynamics]]
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[[Category: actin dynamic]]
[[Category: molecular recognition]]
[[Category: molecular recognition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:55 2008''
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''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

Image:1evh.jpg


PDB ID 1evh

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
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 Thu Mar 20 11:00:49 2008

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