1gc6: Difference between revisions

Revision as of 13:48, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

1GC6 is a Single protein structure of sequence from Mus musculus with as ligand. 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

Page seeded by OCA on Thu Feb 21 12:48:36 2008

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OCA

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-[[Image:1gc6.gif|left|200px]]<br /><applet load="1gc6" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1gc6.gif|left|200px]]<br /><applet load="1gc6" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1gc6, resolution 2.9&Aring;" />
 '''CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN COMPLEXED WITH INOSITOL-(1,4,5)-TRIPHOSPHATE'''<br />
 ==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.
+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==
-GC6 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 I3P as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GC6 OCA].
+GC6 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=I3P:'>I3P</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GC6 OCA].
 ==Reference==
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 [[Category: cytoskeleton]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:55:42 2007''
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