Unknown

Dataset Information

0

Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation.


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.

SUBMITTER: Singh P 

PROVIDER: S-EPMC2376226 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC8607881 | biostudies-literature
| S-EPMC4096112 | biostudies-literature
| S-EPMC3422436 | biostudies-literature
| S-EPMC8958324 | biostudies-literature
| S-EPMC9765450 | biostudies-literature
2009-10-14 | E-GEOD-18292 | biostudies-arrayexpress
| S-EPMC1560097 | biostudies-literature
| S-EPMC3945020 | biostudies-literature
| S-EPMC7196072 | biostudies-literature
| S-EPMC1994991 | biostudies-literature