1NZS: NMR structures of phosphorylated carboxy terminus of bovine rhodopsin in arrestin-bound state

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.
PDB ID: 1NZSDownload
MMDB ID: 74105
PDB Deposition Date: 2003/2/19
Updated in MMDB: 2009/07
Experimental Method:
solution nmr
Similar Structures:
Molecular Components in 1NZS
Label Count Molecule
Protein (1 molecule)
19-mer Peptide Fragment of Rhodopsin(Gene symbol: RHO)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB