1OMW

Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits

Summary for 1OMW

• Entry DOI: 10.2210/pdb1omw/pdb
• Descriptor: G-protein coupled receptor kinase 2, Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit, ... (4 entities in total)
• Functional Keywords: wd-40 repeat, transferase
• Biological source: Bos taurus (cattle); More
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P63212
• Total number of polymer chains: 3
• Total formula weight: 125573.51

Authors

Lodowski, D.T.,Pitcher, J.A.,Capel, W.D.,Lefkowitz, R.J.,Tesmer, J.J.G. (deposition date: 2003-02-26, release date: 2003-06-03, Last modification date: 2023-08-16)

Primary citation

Lodowski, D.T.,Pitcher, J.A.,Capel, W.D.,Lefkowitz, R.J.,Tesmer, J.J.G.
Keeping G proteins at Bay: A Complex Between G Protein-Coupled Receptor Kinase 2 and G-Beta-Gamma
Science, 300:1256-1262, 2003

PubMed Abstract: 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.

PubMed: 12764189
DOI: 10.1126/science.1082348

Experimental method

X-RAY DIFFRACTION (2.5 Å)