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Publication Abstract from PubMed

G protein-coupled receptor kinase 1 (GRK1 or rhodopsin kinase) phosphorylates activated rhodopsin and initiates a cascade of events that results in the termination of phototransduction by the receptor. Although GRK1 seems to be a monomer in solution, seven prior crystal structures of GRK1 revealed a similar domain-swapped dimer interface involving the C-terminus of the enzyme. The influence of this interface on the overall conformation of GRK1 is not known. To address this question, the crystalline dimer interface was disrupted with a L166K mutation and the structure of GRK1-L166K was determined in complex with Mg(2+) . ATP to 2.5 A resolution. GRK1-L166K crystallized in a novel space group as a monomer and exhibited little overall conformational difference from prior structures of GRK1, although the C-terminal domain-swapped region had reorganized owing to loss of the dimer interface.

Structure of a monomeric variant of rhodopsin kinase at 2.5 A resolution.,Tesmer JJ, Nance MR, Singh P, Lee H Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):622-5. doi:, 10.1107/S1744309112017435. Epub 2012 May 22. PMID:22684056^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.