1AZT

GS-ALPHA COMPLEXED WITH GTP-GAMMA-S

1AZT の概要

• エントリーDOI: 10.2210/pdb1azt/pdb
• 分子名称: GS-ALPHA, MAGNESIUM ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, signal transducing protein, gtp-binding protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cell membrane; Lipid-anchor (By similarity): P04896
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96071.64

構造登録者

Tesmer, J.J.G.,Sprang, S.R. (登録日: 1997-11-20, 公開日: 1998-02-25, 最終更新日: 2024-05-22)

主引用文献

Sunahara, R.K.,Tesmer, J.J.,Gilman, A.G.,Sprang, S.R.
Crystal structure of the adenylyl cyclase activator Gsalpha
Science, 278:1943-1947, 1997

PubMed Abstract: The crystal structure of Gsalpha, the heterotrimeric G protein alpha subunit that stimulates adenylyl cyclase, was determined at 2.5 A in a complex with guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS). Gsalpha is the prototypic member of a family of GTP-binding proteins that regulate the activities of effectors in a hormone-dependent manner. Comparison of the structure of Gsalpha.GTPgammaS with that of Gialpha.GTPgammaS suggests that their effector specificity is primarily dictated by the shape of the binding surface formed by the switch II helix and the alpha3-beta5 loop, despite the high sequence homology of these elements. In contrast, sequence divergence explains the inability of regulators of G protein signaling to stimulate the GTPase activity of Gsalpha. The betagamma binding surface of Gsalpha is largely conserved in sequence and structure to that of Gialpha, whereas differences in the surface formed by the carboxyl-terminal helix and the alpha4-beta6 loop may mediate receptor specificity.

PubMed: 9395396
DOI: 10.1126/science.278.5345.1943

実験手法

X-RAY DIFFRACTION (2.3 Å)