1NZS

NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state

Summary for 1NZS

• Entry DOI: 10.2210/pdb1nzs/pdb
• Descriptor: 19-mer peptide fragment of RHODOPSIN (1 entity in total)
• Functional Keywords: rhodopsin, gpcr, arrestin, phosphorylation, helix-loop, ball-and-chain, bound conformation, signal termination, signaling protein
• Cellular location: Membrane; Multi-pass membrane protein: P02699
• Total number of polymer chains: 1
• Total formula weight: 2497.84

Authors

Kisselev, O.G.,McDowell, J.H.,Hargrave, P.A. (deposition date: 2003-02-19, release date: 2004-03-02, Last modification date: 2024-11-13)

Primary citation

Kisselev, O.G.,McDowell, J.H.,Hargrave, P.A.
The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin.
Febs Lett., 564:307-311, 2004

PubMed Abstract: 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.

PubMed: 15111114
DOI: 10.1016/S0014-5793(04)00226-1

Experimental method

SOLUTION NMR