Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X) (PUBMED:7720881), which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction (PUBMED:8452755), (PUBMED:1517224), (PUBMED:2158671).
This C-terminal domain consists of an immunoglobulin-like beta-sandwich structure. This domain is found in arrestins and in other proteins including arrestin domain-containing proteins, protein ROD1 [ (PUBMED:8621680) ] and ROG3 [ (PUBMED:12163175) ] and thioredoxin-interacting protein [ (PUBMED:17603038) ].
Arrestins comprise a family of closely-related proteins. In addition to the inactivation of G protein-coupled receptors, arrestins have been implicated in the endocytosis of receptors and cross talk with other signalling pathways. S-Arrestin (retinal S-antigen) is a major protein of the retinal rod outer segments. It interacts with photo-activated phosphorylated rhodopsin, inhibiting or 'arresting' its ability to interact with transducin [ (PUBMED:15335861) ]. Beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X) [ (PUBMED:7720881) ], which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction [ (PUBMED:8452755) (PUBMED:1517224) (PUBMED:2158671) ]. The crystal structure of bovine retinal arrestin 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 [ (PUBMED:9495348) ].
Family alignment:
There are 9903 Arrestin_C domains in 9566 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Arrestin_C domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Arrestin_C domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Arrestin_C domain in the selected taxonomic class.
The 2.8 A crystal structure of visual arrestin: a model for arrestin'sregulation.
Cell. 1999; 97: 257-69
Display abstract
G protein-coupled signaling is utilized by a wide variety of eukaryotesfor communicating information from the extracellular environment. Signaltermination is achieved by the action of the arrestins, which bind toactivated, phosphorylated G protein-coupled receptors. We describe herecrystallographic studies of visual arrestin in its basal conformation. Thesalient features of the structure are a bipartite molecule with an unusualpolar core. This core is stabilized in part by an extendedcarboxy-terminal tail that locks the molecule into an inactive state. Inaddition, arrestin is found to be a dimer of two asymmetric molecules,suggesting an intrinsic conformational plasticity. In conjunction withbiochemical and mutagenesis data, we propose a molecular mechanism bywhich arrestin is activated for receptor binding.
Transmembrane signal transductions in a variety of cell types that mediatesignals as diverse as those carried by neurotransmitters, hormones, andsensory signals share basic biochemical mechanisms that include: (1) anextracellular perturbation (neurotransmitter, hormone, odor, light); (2)specific receptors; (3) coupling proteins, such as G proteins; and (4)effector enzymes or ion channels. Parallel to these amplificationreactions, receptors are precisely inactivated by mechanisms that involveprotein kinases and regulatory proteins called arrestins. The structureand functions of arrestins are the focus of this review.
