1fqk: Difference between revisions

Revision as of 03:47, 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:1fqk.png

Template:STRUCTURE 1fqk

CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]

Template:ABSTRACT PUBMED 11234020

About this StructureAbout this Structure

1FQK is a Protein complex structure of sequences from Bos taurus and rattus norvegicus and Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A., Slep KC, Kercher MA, He W, Cowan CW, Wensel TG, Sigler PB, Nature. 2001 Feb 22;409(6823):1071-7. PMID:11234020

Page seeded by OCA on Tue Jul 1 03:47:21 2008

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OCA

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-[[Image:1fqk.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1fqk|  PDB=1fqk  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]'''
+===CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]===
-==Overview==
+<!--
-A multitude of heptahelical receptors use heterotrimeric G proteins to transduce signals to specific effector target molecules. The G protein transducin, Gt, couples photon-activated rhodopsin with the effector cyclic GMP phosophodiesterase (PDE) in the vertebrate phototransduction cascade. The interactions of the Gt alpha-subunit (alpha(t)) with the inhibitory PDE gamma-subunit (PDEgamma) are central to effector activation, and also enhance visual recovery in cooperation with the GTPase-activating protein regulator of G-protein signalling (RGS)-9 (refs 1-3). Here we describe the crystal structure at 2.0 A of rod transducin alpha x GDP x AlF4- in complex with the effector molecule PDEgamma and the GTPase-activating protein RGS9. In addition, we present the independently solved crystal structures of the RGS9 RGS domain both alone and in complex with alpha(t/i1) x GDP x AlF4-. These structures reveal insights into effector activation, synergistic GTPase acceleration, RGS9 specificity and RGS activity. Effector binding to a nucleotide-dependent site on alpha(t) sequesters PDEgamma residues implicated in PDE inhibition, and potentiates recruitment of RGS9 for hydrolytic transition state stabilization and concomitant signal termination.
+The line below this paragraph, {{ABSTRACT_PUBMED_11234020}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11234020 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11234020}}
 ==About this Structure==
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 [[Category: Rod]]
 [[Category: Transducin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:38:54 2008''
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