title: X-ray crystal structure of arrestin from bovine rod outer segments.
abstract: 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.
authors.affiliation: Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung, Germany. J.Granzin@fz-juelich.de
authors.forename: J
authors.initials: J
authors.lastname: Granzin
authors.forename: U
authors.initials: U
authors.lastname: Wilden
authors.forename: H W
authors.initials: HW
authors.lastname: Choe
authors.forename: J
authors.initials: J
authors.lastname: Labahn
authors.forename: B
authors.initials: B
authors.lastname: Krafft
authors.forename: G
authors.initials: G
authors.lastname: Büldt
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019393:Arrestin / Q000737:chemistry* / Q000302:isolation & purification; D001665:Binding Sites; D002417:Cattle; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012374:Rod Cell Outer Segment / Q000737:chemistry*
chemical_list: D019393:Arrestin