1nzs
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(New page: 200px<br /><applet load="1nzs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nzs" /> '''NMR structures of phosphorylated carboxy ter...)
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Revision as of 20:34, 20 November 2007
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NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state
Overview
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.
About this Structure
1NZS is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 22:41:37 2007
