1VQX

ARRESTIN-BOUND NMR STRUCTURES OF THE PHOSPHORYLATED CARBOXY-TERMINAL DOMAIN OF RHODOPSIN, REFINED

「1TQK」から置き換えられました

1VQX の概要

• エントリーDOI: 10.2210/pdb1vqx/pdb
• 関連するPDBエントリー: 1NZS
• 分子名称: RHODOPSIN (1 entity in total)
• 機能のキーワード: helix-loop, signaling protein
• 細胞内の位置: Membrane; Multi-pass membrane protein: P02699
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2497.84

構造登録者

Kisselev, O.G.,Downs, M.A.,Mcdowell, J.H.,Hargrave, P.A. (登録日: 2005-01-07, 公開日: 2005-01-18, 最終更新日: 2024-10-09)

主引用文献

Kisselev, O.G.,Downs, M.A.,Mcdowell, J.H.,Hargrave, P.A.
Conformational Changes in the Phosphorylated C-Terminal Domain of Rhodopsin During Rhodopsin Arrestin Interactions
J.Biol.Chem., 279:51203-, 2004

PubMed Abstract: Phosphorylation of activated G-protein-coupled receptors and the subsequent binding of arrestin mark major molecular events of homologous desensitization. In the visual system, interactions between arrestin and the phosphorylated rhodopsin are pivotal for proper termination of visual signals. By using high resolution proton nuclear magnetic resonance spectroscopy of the phosphorylated C terminus of rhodopsin, represented by a synthetic 7-phosphopolypeptide, we show that the arrestin-bound conformation is a well ordered helix-loop structure connected to rhodopsin via a flexible linker. In a model of the rhodopsin-arrestin complex, the phosphates point in the direction of arrestin and form a continuous negatively charged surface, which is stabilized by a number of positively charged lysine and arginine residues of arrestin. Opposite to the mostly extended structure of the unphosphorylated C-terminal domain of rhodopsin, the arrestin-bound C-terminal helix is a compact domain that occupies a central position between the cytoplasmic loops and occludes the key binding sites of transducin. In conjunction with other binding sites, the helix-loop structure provides a mechanism of shielding phosphates in the center of the rhodopsin-arrestin complex and appears critical in guiding arrestin for high affinity binding with rhodopsin.

PubMed: 15351781
DOI: 10.1074/jbc.M407341200

実験手法

SOLUTION NMR