1gc7: Difference between revisions

Revision as of 05:04, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1gc7.png

Template:STRUCTURE 1gc7

CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAINCRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN

Template:ABSTRACT PUBMED 10970839

About this StructureAbout this Structure

1GC7 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain., Hamada K, Shimizu T, Matsui T, Tsukita S, Hakoshima T, EMBO J. 2000 Sep 1;19(17):4449-62. PMID:10970839

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OCA

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-'''CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN'''
+===CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN===
-==Overview==
+<!--
-Radixin is a member of the ezrin/radixin/moesin (ERM) family of proteins, which play a role in the formation of the membrane-associated cytoskeleton by linking actin filaments and adhesion proteins. This cross-linking activity is regulated by phosphoinositides such as phosphatidylinositol 4,5-bisphosphate (PIP2) in the downstream of the small G protein Rho. The X-ray crystal structures of the radixin FERM domain, which is responsible for membrane binding, and its complex with inositol-(1,4, 5)-trisphosphate (IP3) have been determined. The domain consists of three subdomains featuring a ubiquitin-like fold, a four-helix bundle and a phosphotyrosine-binding-like domain, respectively. These subdomains are organized by intimate interdomain interactions to form characteristic grooves and clefts. One such groove is negatively charged and so is thought to interact with basic juxta-membrane regions of adhesion proteins. IP3 binds a basic cleft that is distinct from those of pleckstrin homology domains and is located on a positively charged flat molecular surface, suggesting an electrostatic mechanism of plasma membrane targeting. Based on the structural changes associated with IP3 binding, a possible unmasking mechanism of ERM proteins by PIP2 is proposed.
+The line below this paragraph, {{ABSTRACT_PUBMED_10970839}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10970839 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10970839}}
 ==About this Structure==
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 [[Category: 3 subdomains,cytoskeleton]]
 [[Category: Cell adhesion]]
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