Structure of a monomeric variant of rhodopsin kinase at 2.5 Å resolution

John J.G. Tesmer, Mark R. Nance, Puja Singh, Harie Lee

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

G protein-coupled receptor kinase 1 (GRK1 or rhodopsin kinase) phosphoryl-ates 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 Å 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.

Original languageEnglish (US)
Pages (from-to)622-625
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number6
DOIs
StatePublished - May 2012

Keywords

  • GRK1
  • RGS homology domain
  • dimerization
  • rhodopsin kinase

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