3c4y: Difference between revisions

Revision as of 16:00, 29 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:3c4y.png

Template:STRUCTURE 3c4y

Crystal Structure of Apo form of G protein coupled receptor kinase 1 at 7.51ACrystal Structure of Apo form of G protein coupled receptor kinase 1 at 7.51A

Template:ABSTRACT PUBMED 18339619

About this StructureAbout this Structure

3C4Y is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structures of Rhodopsin Kinase in Different Ligand States Reveal Key Elements Involved in G Protein-coupled Receptor Kinase Activation., Singh P, Wang B, Maeda T, Palczewski K, Tesmer JJ, J Biol Chem. 2008 May 16;283(20):14053-62. Epub 2008 Mar 13. PMID:18339619

Page seeded by OCA on Tue Jul 29 16:00:18 2008

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OCA

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-'''Crystal Structure of Apo form of G protein coupled receptor kinase 1 at 7.51A'''
+===Crystal Structure of Apo form of G protein coupled receptor kinase 1 at 7.51A===
-==Overview==
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-G protein-coupled receptor (GPCR) kinases (GRKs) phosphorylate activated heptahelical receptors, leading to their uncoupling from G proteins. Here we report six crystal structures of rhodopsin kinase (GRK1), revealing not only three distinct nucleotide-binding states of a GRK but also two key structural elements believed to be involved in the recognition of activated GPCRs. The first is the C-terminal extension of the kinase domain, which was observed in all nucleotide-bound GRK1 structures. The second is residues 5-30 of the N terminus, observed in one of the GRK1.(Mg(2+))(2).ATP structures. The N terminus was also clearly phosphorylated, leading to the identification of two novel phosphorylation sites by mass spectral analysis. Co-localization of the N terminus and the C-terminal extension near the hinge of the kinase domain suggests that activated GPCRs stimulate kinase activity by binding to this region to facilitate full closure of the kinase domain.
+The line below this paragraph, {{ABSTRACT_PUBMED_18339619}}, adds the Publication Abstract to the page
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 [[Category: Serine/threonine-protein kinase]]
 [[Category: Transferase]]
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