1gwn: Difference between revisions

Revision as of 06:13, 1 July 2008

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File:1gwn.png

Template:STRUCTURE 1gwn

THE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3- A CONSTITUTIVELY ACTIVATED SMALL G PROTEINTHE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3- A CONSTITUTIVELY ACTIVATED SMALL G PROTEIN

Template:ABSTRACT PUBMED 12009891

About this StructureAbout this Structure

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

ReferenceReference

Crystal structure of the core domain of RhoE/Rnd3: a constitutively activated small G protein., Garavini H, Riento K, Phelan JP, McAlister MS, Ridley AJ, Keep NH, Biochemistry. 2002 May 21;41(20):6303-10. PMID:12009891

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OCA

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-'''THE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3- A CONSTITUTIVELY ACTIVATED SMALL G PROTEIN'''
+===THE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3- A CONSTITUTIVELY ACTIVATED SMALL G PROTEIN===
-==Overview==
+<!--
-We report the 2.1 A crystal structure of the core G protein domain of the unusual Rho family member RhoE/Rnd3 in complex with endogenous GTP and magnesium. Unlike other small G proteins, RhoE, along with two other proteins Rnd1/Rho6 and Rnd2/RhoN, does not hydrolyze GTP. The main reason for this is the presence of serines in the positions equivalent to Ala59 and Gln61 in Ras. The structure shows that there are still water molecules in similar positions to the waters thought to be involved in the hydrolysis reaction in other G proteins. The structure suggests three not necessarily exclusive explanations for the lack of hydrolysis. The lack of the conserved glutamine raises the energy of the transition state inhibiting hydrolysis. The serines may restrain the waters from moving closer to the GTP, a step that is required to attain the transition state. They also stabilize the GTP-bound conformation of switch II and could prevent conformational changes required during hydrolysis. By superposition of the RhoE structure on structures of Rho family proteins in complex with binding partners, we make predictions on RhoE interactions with these partners.
+The line below this paragraph, {{ABSTRACT_PUBMED_12009891}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12009891 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12009891}}
 ==About this Structure==
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 [[Category: Inactive gtpase]]
 [[Category: Signal transduction]]
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