X-ray crystal structure of arrestin from bovine rod outer segments

Nature. 1998 Feb 26;391(6670):918-21. doi: 10.1038/36147.


Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 A resolution. The crystal structure comprises two domains of antiparallel beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arrestin / chemistry*
  • Arrestin / isolation & purification
  • Binding Sites
  • Cattle
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Conformation
  • Protein Structure, Secondary
  • Rod Cell Outer Segment / chemistry*


  • Arrestin

Associated data

  • PDB/1AYR