The arrestin‐bound conformation and dynamics of the phosphorylated carboxy‐terminal region of rhodopsin

FEBS Letters

Hargrave, Paul A.¹  McDowell, J.Hugh¹  Kisselev, Oleg G.² 

[1] Department of Ophthalmology, University of Florida, Gainesville, FL, USA;Departments of Ophthalmology and Biochemistry and Molecular Biology, Saint Louis University School of Medicine, 1755 S. Grand Blvd., St. Louis, MO 63104, USA

关键词: Rhodopsin;    Arrestin;    Phosphorylation;    Signal termination;    Nuclear magnetic resonance;   

DOI  :  10.1016/S0014-5793(04)00226-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Visual arrestin binds to the phosphorylated carboxy-terminal region of rhodopsin to block interactions with transducin and terminate signaling in the rod photoreceptor cells. A synthetic seven-phospho-peptide from the C-terminal region of rhodopsin, Rh(330–348), has been shown to bind arrestin and mimic inhibition of signal transduction. In this study, we examine conformational changes in this synthetic peptide upon binding to arrestin by high-resolution proton nuclear magnetic resonance (NMR). We show that the peptide is completely disordered in solution, but becomes structured upon binding to arrestin. A control, unphosphorylated peptide that fails to bind to arrestin remains highly disordered. Specific NMR distance constraints are used to model the arrestin-bound conformation. The models suggest that the phosphorylated carboxy-terminal region of rhodopsin, Rh(330–348), undergoes significant conformational changes and becomes structured upon binding to arrestin.

【 授权许可】

Unknown