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.
Publication Abstract from PubMed
Visual arrestin specifically binds to photoactivated and phosphorylated rhodopsin and inactivates phototransduction. In contrast, the p44 splice variant can terminate phototransduction by binding to nonphosphorylated light-activated rhodopsin. Here we report the crystal structure of bovine p44 at a resolution of 1.85 A. Compared to native arrestin, the p44 structure reveals significant differences in regions crucial for receptor binding, namely flexible loop V-VI and polar core regions. Additionally, electrostatic potential is remarkably positive on the N-domain and the C-domain. The p44 structure represents an active conformation that serves as a model to explain the 'constitutive activity' found in arrestin variants.
Crystal Structure of p44, a Constitutively Active Splice Variant of Visual Arrestin.,Granzin J, Cousin A, Weirauch M, Schlesinger R, Buldt G, Batra-Safferling R J Mol Biol. 2012 Mar 9;416(5):611-8. Epub 2012 Jan 27. PMID:22306737[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Granzin J, Cousin A, Weirauch M, Schlesinger R, Buldt G, Batra-Safferling R. Crystal Structure of p44, a Constitutively Active Splice Variant of Visual Arrestin. J Mol Biol. 2012 Mar 9;416(5):611-8. Epub 2012 Jan 27. PMID:22306737 doi:10.1016/j.jmb.2012.01.028
