1CF1
ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
Summary for 1CF1
| Entry DOI | 10.2210/pdb1cf1/pdb |
| Descriptor | PROTEIN (ARRESTIN) (2 entities in total) |
| Functional Keywords | visual arrestin, desensitisation of the visual transduction cascade, binding to acticated and phosphorylated rhodopsin, structural protein |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 4 |
| Total formula weight | 181042.55 |
| Authors | Hirsch, J.A.,Schubert, C.,Gurevich, V.V.,Sigler, P.B. (deposition date: 1999-03-23, release date: 1999-04-16, Last modification date: 2023-12-27) |
| Primary citation | Hirsch, J.A.,Schubert, C.,Gurevich, V.V.,Sigler, P.B. The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation. Cell(Cambridge,Mass.), 97:257-269, 1999 Cited by PubMed Abstract: G protein-coupled signaling is utilized by a wide variety of eukaryotes for communicating information from the extracellular environment. Signal termination is achieved by the action of the arrestins, which bind to activated, phosphorylated G protein-coupled receptors. We describe here crystallographic studies of visual arrestin in its basal conformation. The salient features of the structure are a bipartite molecule with an unusual polar core. This core is stabilized in part by an extended carboxy-terminal tail that locks the molecule into an inactive state. In addition, arrestin is found to be a dimer of two asymmetric molecules, suggesting an intrinsic conformational plasticity. In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding. PubMed: 10219246DOI: 10.1016/S0092-8674(00)80735-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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