1evh: Difference between revisions
New page: left|200px<br /><applet load="1evh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1evh, resolution 1.8Å" /> '''EVH1 DOMAIN FROM MURI... |
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[[Image:1evh.jpg|left|200px]]<br /><applet load="1evh" size=" | [[Image:1evh.jpg|left|200px]]<br /><applet load="1evh" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1evh, resolution 1.8Å" /> | caption="1evh, resolution 1.8Å" /> | ||
'''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE'''<br /> | '''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
The Enabled/VASP homology 1 (EVH1; also called WH1) domain is an | 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== | ==About this Structure== | ||
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 ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lee, D | [[Category: Lee, D J.]] | ||
[[Category: Lim, W | [[Category: Lim, W A.]] | ||
[[Category: Prehoda, K | [[Category: Prehoda, K E.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: actin dynamics]] | [[Category: actin dynamics]] | ||
[[Category: molecular recognition]] | [[Category: molecular recognition]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:55 2008'' | ||
Revision as of 10:31, 21 February 2008
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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 with ACE as ligand. 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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