Publication Abstract from PubMed
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.
The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin.,Kisselev OG, McDowell JH, Hargrave PA FEBS Lett. 2004 Apr 30;564(3):307-11. PMID:15111114[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
