1evh: Difference between revisions

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[[Image:1evh.~~jpg~~|left|200px]]

[[Image:1evh.png|left|200px]]

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~~'''~~EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE~~'''~~

===EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_10338211}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10338211 is the PubMed ID number.

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==About this Structure==

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[[Category: Actin dynamic]]

[[Category: Molecular recognition]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:33:56 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:05:00 2008''

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-[[Image:1evh.jpg|left|200px]]
+{{Seed}}
+[[Image:1evh.png|left|200px]]
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 {{STRUCTURE_1evh|  PDB=1evh  |  SCENE=  }}
-'''EVH1 DOMAIN FROM MURINE ENABLED IN COMPLEX WITH ACTA PEPTIDE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10338211}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10338211 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10338211}}
 ==About this Structure==
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 [[Category: Actin dynamic]]
 [[Category: Molecular recognition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:33:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:05:00 2008''