2bcj
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(New page: 200px<br /><applet load="2bcj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bcj, resolution 3.061Å" /> '''Crystal Structure o...)
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Revision as of 06:36, 21 November 2007
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Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits
Overview
G protein-coupled receptor kinase 2 (GRK2) plays a key role in the, desensitization of G protein-coupled receptor signaling by phosphorylating, activated heptahelical receptors and by sequestering heterotrimeric G, proteins. We report the atomic structure of GRK2 in complex with Galphaq, and Gbetagamma, in which the activated Galpha subunit of Gq is fully, dissociated from Gbetagamma and dramatically reoriented from its position, in the inactive Galphabetagamma heterotrimer. Galphaq forms an, effector-like interaction with the GRK2 regulator of G protein signaling, (RGS) homology domain that is distinct from and does not overlap with that, used to bind RGS proteins such as RGS4.
About this Structure
2BCJ is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus,mus musculus with MG, ALF, ACE and GDP as ligands. Active as [Beta-adrenergic-receptor_kinase [Beta-adrenergic-receptor] kinase], with EC number 2.7.11.15 Full crystallographic information is available from OCA.
Reference
Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex., Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, Tesmer JJ, Science. 2005 Dec 9;310(5754):1686-90. PMID:16339447[[Category: [Beta-adrenergic-receptor] kinase]]
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