3C4X

Crystal Structure of G protein coupled receptor kinase 1 bound to ATP and magnesium chloride at 2.9A

Summary for 3C4X

• Entry DOI: 10.2210/pdb3c4x/pdb
• Related: 3C4W 3C4Y 3C4Z 3C50 3C51
• Descriptor: Rhodopsin kinase, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: ser/thr kinase, rgs homology domain, g protein coupled receptor kinase, grk, grk1, rhodopsin kinase, p-loop, autophosphorylation, atp-binding, lipoprotein, membrane, methylation, nucleotide-binding, phosphoprotein, prenylation, serine/threonine-protein kinase, transferase
• Biological source: Bos taurus (cattle)
• Cellular location: Membrane; Lipid-anchor: P28327
• Total number of polymer chains: 2
• Total formula weight: 123993.75

Authors

Singh, P.,Tesmer, J.J.G. (deposition date: 2008-01-30, release date: 2008-03-11, Last modification date: 2023-08-30)

Primary citation

Singh, P.,Wang, B.,Maeda, T.,Palczewski, K.,Tesmer, J.J.
Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation.
J.Biol.Chem., 283:14053-14062, 2008

PubMed Abstract: 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.(Mg2+)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.

PubMed: 18339619
DOI: 10.1074/jbc.M708974200

Experimental method

X-RAY DIFFRACTION (2.9 Å)