1gc6

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|RELATEDENTRY=[[1ef1|1EF1]], [[1gc7|1GC7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gc6 OCA], [http://www.ebi.ac.uk/pdbsum/1gc6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gc6 RCSB]</span>
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[[Category: Shimizu, T.]]
[[Category: Shimizu, T.]]
[[Category: Tsukita, S.]]
[[Category: Tsukita, S.]]
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[[Category: I3P]]
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[[Category: cytoskeleton,cell adhesion]]
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[[Category: cell adhesion]]
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[[Category: cytoskeleton]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:10 2008''

Revision as of 17:41, 30 March 2008


PDB ID 1gc6

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands:
Related: 1EF1, 1GC7


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN COMPLEXED WITH INOSITOL-(1,4,5)-TRIPHOSPHATE


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.

About this Structure

1GC6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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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