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Solution NMR

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

Released:
DOI: 10.2210/pdb1nzs/pdb
PDB entry 1nzs coloured by chain, ensemble of 16 models, front view.
PDB entry 1nzs coloured by chain, ensemble of 16 models, side view.
PDB entry 1nzs coloured by chain, ensemble of 16 models, top view.
Source organism: Bos taurus
Primary publication:
The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin.
Kisselev OG, McDowell JH, Hargrave PA
FEBS Lett 564 307-11 (2004)
PMID: 15111114

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136065 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhodopsin Chain: A
Molecule details ›
Chain: A
Length: 19 amino acids
Theoretical weight: 2.5 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P02699 (Residues: 330-348; Coverage: 6%)
Gene name: RHO

Ligands and Environments

No bound ligands
2 modified residues:
Ligand SEP 3 x SEP
Ligand TPO 4 x TPO

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, constrained molecular dynamics, simulated annealing
Expression system: Not provided

Quick links

Citations

2 review citations

The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling.
Peterson et al. (2017)
1 more

2 mentions without citation

Unraveling the structure and function of G protein-coupled receptors through NMR spectroscopy.
Tikhonova et al. (2009)
1 more