Rhodopsin kinase

From Proteopedia

Bovine rhodopsin kinase complex with ATP, Mg+2 and Cl- ions (PDB code 3c4x) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Rhodopsin kinase (RK) is an enzyme which catalyzes the conversion of rhodopsin and ATP to phosphorhodopsin and ADP. RK is retina-specific and the phosphorylation of rhodopsin initiates the phototransduction cascade[1]. The rapid desensitization permits rapid adaptation to changes in illumination. RK is inhibited by the neuronal calcium-binding protein recoverin. Disease Mutations in RK are associated with night blindness[2]. Structural highlights The active site of RK is located between its and [3]. An . Water molecules are shown as red spheres.

3D Structures of rhodopsin kinase

Updated on 17-October-2023

3c4y – bRK – bovine
3t8o – bRK (mutant)
3c4w, 3c4x – bRK + ATP
3c4z, 3c50, 3c51 – bRK + ADP
3qc9 – bRK (mutant) + ADP
4l9i – bRK + paroxetine
4pni – bRK + inhibitor
4wbo – bRK + almexanox
2i94 – bRK + recoverin - NMR
7mt9 – bRK + rhodpsin + retinal – Cryo EM
7mtb – bRK (mutant) + rhodpsin + retinal – Cryo EM
7mta – bRK (mutant) + rhodpsin + retinal + antibody – Cryo EM
7mt8 – bRK (mutant) + rhodpsin + retinal + antibiotic – Cryo EM

References

1. ↑ Kuhn H, Wilden U. Deactivation of photoactivated rhodopsin by rhodopsin-kinase and arrestin. J Recept Res. 1987;7(1-4):283-98. PMID:3040978
2. ↑ Yamamoto S, Sippel KC, Berson EL, Dryja TP. Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness. Nat Genet. 1997 Feb;15(2):175-8. PMID:9020843 doi:http://dx.doi.org/10.1038/ng0297-175
3. ↑ Singh P, Wang B, Maeda T, Palczewski K, Tesmer JJ. Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation. J Biol Chem. 2008 May 16;283(20):14053-62. Epub 2008 Mar 13. PMID:18339619 doi:10.1074/jbc.M708974200