Sandbox 173: Difference between revisions

Rhodopsin kinase phosphorylates rhodopsin and arrestin binds to the phosphorylated domain of rhodopsin, preventing further signal transduction from Metarhodopsin II of activated rhodopsin and transducin<ref>Article 3</ref>. It phosphorylates both Metarhodopsin II and cone opsins. The majority of the phosphorylation sites are in the cytoplasmic C-terminal region of rhodopsin with seven hydroxy-amino acids. The most favoured amino acids were <scene name='Sandbox_173/Phosphorylated_sites/1'>Serine 338, Serine 343, Serine 334, Threonine 335 and Threonine 336</scene><ref>Article 7</ref>. These residues form an arrangement in rhodopsin that does not appear to be exposed to the solvent. Interactions with the C-terminal tail and a portion of the Cytoplasmic loop 3 appear to be broken for the phosphorylation of the hydroxyl groups<ref>Article 9</ref>. For the next cycle of activation of rhodopsin, rhodopsin has to be dephosphorylated, and have the all-''trans'' retinal replaced with the 11-''cis'' retinal<ref>Article 19</ref>.