3T8O

Structure of a monomeric variant of rhodopsin kinase at 2.5 A resolution.

(2012) Acta Crystallogr Sect F Struct Biol Cryst Commun 68: 622-625

• PubMed: 22684056 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S1744309112017435
• Primary Citation of Related Structures:  
  3T8O


• PubMed Abstract: 
  

  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 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.

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Organizational Affiliation: 

Life Sciences Institute and the Department of Pharmacology, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, MI 48109-2216, USA. tesmerjj@umich.edu