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Nature. 1998 Feb 26;391(6670):918-21.

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

Author information

1
Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung, Germany. J.Granzin@fz-juelich.de

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.

PMID:
9495348
DOI:
10.1038/36147
[Indexed for MEDLINE]

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