1AYR

ARRESTIN FROM BOVINE ROD OUTER SEGMENTS

1AYR の概要

• エントリーDOI: 10.2210/pdb1ayr/pdb
• 分子名称: ARRESTIN (2 entities in total)
• 機能のキーワード: sensory transduction, arrestin, rhodopsin
• 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: 164005.09

構造登録者

Granzin, J.,Wilden, U.,Choe, H.-W.,Labahn, J.,Krafft, B.,Bueldt, G. (登録日: 1997-11-10, 公開日: 1998-11-25, 最終更新日: 2024-02-07)

主引用文献

Granzin, J.,Wilden, U.,Choe, H.W.,Labahn, J.,Krafft, B.,Buldt, G.
X-ray crystal structure of arrestin from bovine rod outer segments.
Nature, 391:918-921, 1998

PubMed Abstract: Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 A resolution. The crystal structure comprises two domains of antiparallel beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin.

PubMed: 9495348
DOI: 10.1038/36147

実験手法

X-RAY DIFFRACTION (3.3 Å)