Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state.

@article{Gurevich1997MechanismOP,
  title={Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state.},
  author={Vsevolod V. Gurevich and Jeffrey L. Benovic},
  journal={Molecular pharmacology},
  year={1997},
  volume={51 1},
  pages={
          161-9
        }
}
Arrestin plays an important role in quenching phototransduction via its ability to interact specifically with the phosphorylated light-activated form of the visual receptor rhodopsin (P-Rh*). Previous studies have demonstrated that Arg175 in bovine arrestin is directly involved in the phosphorylation-dependent binding of arrestin to rhodopsin and seems to function as a phosphorylation-sensitive trigger. In this study, we further probed the molecular mechanism of phosphorylation recognition by… CONTINUE READING

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