1agr: Difference between revisions

Revision as of 16:49, 30 June 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:1agr.png

Template:STRUCTURE 1agr

COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4

Template:ABSTRACT PUBMED 9108480

About this StructureAbout this Structure

1AGR is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis., Tesmer JJ, Berman DM, Gilman AG, Sprang SR, Cell. 1997 Apr 18;89(2):251-61. PMID:9108480

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OCA

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-'''COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4'''
+===COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4===
-==Overview==
+<!--
-RGS proteins are GTPase activators for heterotrimeric G proteins. We report here the 2.8 A resolution crystal structure of the RGS protein RGS4 complexed with G(i alpha1)-Mg2+-GDP-AlF4 . Only the core domain of RGS4 is visible in the crystal. The core domain binds to the three switch regions of G(i alpha1), but does not contribute catalytic residues that directly interact with either GDP or AlF4-. Therefore, RGS4 appears to catalyze rapid hydrolysis of GTP primarily by stabilizing the switch regions of G(i alpha1), although the conserved Asn-128 from RGS4 could also play a catalytic role by interacting with the hydrolytic water molecule or the side chain of Gln-204. The binding site for RGS4 on G(i alpha1) is also consistent with the activity of RGS proteins as antagonists of G(alpha) effectors.
+The line below this paragraph, {{ABSTRACT_PUBMED_9108480}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9108480 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9108480}}
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 [[Category: Rgs4]]
 [[Category: Signal transduction]]
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