1CF1

ARRESTIN FROM BOVINE ROD OUTER SEGMENTS

1CF1 の概要

• エントリーDOI: 10.2210/pdb1cf1/pdb
• 分子名称: PROTEIN (ARRESTIN) (2 entities in total)
• 機能のキーワード: visual arrestin, desensitisation of the visual transduction cascade, binding to acticated and phosphorylated rhodopsin, structural protein
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 181042.55

構造登録者

Hirsch, J.A.,Schubert, C.,Gurevich, V.V.,Sigler, P.B. (登録日: 1999-03-23, 公開日: 1999-04-16, 最終更新日: 2023-12-27)

主引用文献

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

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: 10219246
DOI: 10.1016/S0092-8674(00)80735-7

実験手法

X-RAY DIFFRACTION (2.8 Å)