7F1X

X-ray crystal structure of visual arrestin complexed with inositol 1,4,5-triphosphate

7F1X の概要

• エントリーDOI: 10.2210/pdb7f1x/pdb
• 分子名称: S-arrestin, D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE, PENTANEDIAL, ... (5 entities in total)
• 機能のキーワード: signaling protein
• 由来する生物種: Bos taurus (Bovine)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 183381.92

構造登録者

Jang, K.,Kang, M.,Eger, B.T.,Choe, H.W.,Ernst, O.P.,Kim, Y.J. (登録日: 2021-06-10, 公開日: 2021-10-27, 最終更新日: 2023-11-29)

主引用文献

Sander, C.L.,Luu, J.,Kim, K.,Furkert, D.,Jang, K.,Reichenwallner, J.,Kang, M.,Lee, H.J.,Eger, B.T.,Choe, H.W.,Fiedler, D.,Ernst, O.P.,Kim, Y.J.,Palczewski, K.,Kiser, P.D.
Structural evidence for visual arrestin priming via complexation of phosphoinositols.
Structure, 30:263-277.e5, 2022

PubMed Abstract: Visual arrestin (Arr1) terminates rhodopsin signaling by blocking its interaction with transducin. To do this, Arr1 translocates from the inner to the outer segment of photoreceptors upon light stimulation. Mounting evidence indicates that inositol phosphates (InsPs) affect Arr1 activity, but the Arr1-InsP molecular interaction remains poorly defined. We report the structure of bovine Arr1 in a ligand-free state featuring a near-complete model of the previously unresolved C-tail, which plays a crucial role in regulating Arr1 activity. InsPs bind to the N-domain basic patch thus displacing the C-tail, suggesting that they prime Arr1 for interaction with rhodopsin and help direct Arr1 translocation. These structures exhibit intact polar cores, suggesting that C-tail removal by InsP binding is insufficient to activate Arr1. These results show how Arr1 activity can be controlled by endogenous InsPs in molecular detail.

PubMed: 34678158
DOI: 10.1016/j.str.2021.10.002

実験手法

X-RAY DIFFRACTION (3 Å)