2BCJ

Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits

Summary for 2BCJ

• Entry DOI: 10.2210/pdb2bcj/pdb
• Related: 1OMW 1YM7
• Descriptor: G-protein-coupled receptor kinase 2, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (8 entities in total)
• Functional Keywords: peripheral membrane complex, protein kinase, rgs domain, wd40 protein, heterotrimeric g protein, transferase-hydrolase complex, transferase/hydrolase
• Biological source: Bos taurus (Bovine); More
• Cellular location: Cytoplasm : P21146; Cell membrane ; Lipid-anchor ; Cytoplasmic side : P63212; Nucleus : P21279
• Total number of polymer chains: 4
• Total formula weight: 166776.15

Authors

Tesmer, J.J.G. (deposition date: 2005-10-19, release date: 2005-12-20, Last modification date: 2024-10-16)

Primary citation

Tesmer, V.M.,Kawano, T.,Shankaranarayanan, A.,Kozasa, T.,Tesmer, J.J.G.
Snapshot of Activated G Proteins at the Membrane: The Gq-GRK2-G Complex
Science, 310:1686-1690, 2005

PubMed Abstract: 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.

PubMed: 16339447
DOI: 10.1126/science.1118890

Experimental method

X-RAY DIFFRACTION (3.061 Å)