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The arrestin‐bound conformation and dynamics of the phosphorylated carboxy‐terminal region of rhodopsin
Author(s) -
Kisselev Oleg G.,
McDowell J.Hugh,
Hargrave Paul A.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00226-1
Subject(s) - rhodopsin , terminal (telecommunication) , phosphorylation , arrestin , chemistry , biophysics , microbiology and biotechnology , dynamics (music) , biochemistry , biology , g protein coupled receptor , receptor , physics , computer science , retinal , telecommunications , acoustics
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.