1omw
|
Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits
OverviewOverview
The phosphorylation of heptahelical receptors by heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptor kinases (GRKs) is a universal regulatory mechanism that leads to desensitization of G protein signaling and to the activation of alternative signaling pathways.We determined the crystallographic structure of bovine GRK2 in complex with G protein beta1gamma2 subunits.Our results show how the three domains of GRK2-the RGS (regulator of G protein signaling) homology, protein kinase, and pleckstrin homology domains-integrate their respective activities and recruit the enzyme to the cell membrane in an orientation that not only facilitates receptor phosphorylation, but also allows for the simultaneous inhibition of signaling by Galpha and Gbetagamma subunits.
About this StructureAbout this Structure
1OMW is a Protein complex structure of sequences from Bos taurus. Active as [Beta-adrenergic-receptor_kinase [Beta-adrenergic-receptor] kinase], with EC number 2.7.11.15 Full crystallographic information is available from OCA.
ReferenceReference
Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma., Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ, Science. 2003 May 23;300(5623):1256-62. PMID:12764189 [[Category: [Beta-adrenergic-receptor] kinase]]
Page seeded by OCA on Thu Feb 21 14:19:24 2008