Structural highlights
Disease
[ARRS_BOVIN] Note=S-antigen induces autoimmune uveitis.
Function
[ARRS_BOVIN] Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
X-ray crystal structure of arrestin from bovine rod outer segments.,Granzin J, Wilden U, Choe HW, Labahn J, Krafft B, Buldt G Nature. 1998 Feb 26;391(6670):918-21. PMID:9495348[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Granzin J, Wilden U, Choe HW, Labahn J, Krafft B, Buldt G. X-ray crystal structure of arrestin from bovine rod outer segments. Nature. 1998 Feb 26;391(6670):918-21. PMID:9495348 doi:10.1038/36147
