Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 283, Issue 20, Pages 14053-14062Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M708974200
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Funding
- NCI NIH HHS [Y1-CO-1020] Funding Source: Medline
- NEI NIH HHS [R01 EY008061, P30-EY11373, R01 EY008061-22, P30 EY011373, EY 08061, P30 EY011373-129005] Funding Source: Medline
- NHLBI NIH HHS [HL071818] Funding Source: Medline
- NIGMS NIH HHS [Y1-GM-1104] Funding Source: Medline
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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 center dot(Mg2+)(2)center dot 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.
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