| | |  | | | | Record from Web of Science® | | | | | | |
| The 2.8 angstrom crystal structure of visual arrestin: A model for arrestin's regulation |
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| Author(s): Hirsch JA, Schubert C, Gurevich VV, Sigler PB |
| Source: CELL Volume: 97 Issue: 2 Pages: 257-269 Published: APR 16 1999 |
| Times Cited: 151 References: 61 |
| 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: Sigler, PB (reprint author), Yale Univ, Howard Hughes Med Inst, New Haven, CT 06511 USA |
Addresses:
1. Yale Univ, Howard Hughes Med Inst, New Haven, CT 06511 USA
2. Yale Univ, Dept Biochem & Mol Biophys, New Haven, CT 06511 USA
3. Sun Hlth Res Inst, Ralph & Muriel Roberts Lab Vis Sci, Sun City, AZ 85372 USA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 USA |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: 187GY |
| ISSN: 0092-8674 |
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