2TRC

PHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX

2TRC の概要

• エントリーDOI: 10.2210/pdb2trc/pdb
• 分子名称: TRANSDUCIN, PHOSDUCIN, GADOLINIUM ATOM, ... (5 entities in total)
• 機能のキーワード: phosducin, transducin, beta-gamma, signal transduction, regulation, phosphorylation, g proteins, thioredoxin, vision, meka, complex (transducer-transduction), complex (transducer-transduction) complex, complex (transducer/transduction)
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 71345.91

構造登録者

Gaudet, R.,Bohm, A.,Sigler, P.B. (登録日: 1997-01-06, 公開日: 1997-06-05, 最終更新日: 2024-11-20)

主引用文献

Gaudet, R.,Bohm, A.,Sigler, P.B.
Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin.
Cell(Cambridge,Mass.), 87:577-588, 1996

PubMed Abstract: The crystal structure of transducin's betagamma subunits complexed with phosducin, which regulates Gtbetagamma activity, has been solved to 2.4 angstroms resolution. Phosducin has two domains that wrap around Gtbetagamma to form an extensive interface. The N-terminal domain binds loops on the "top" Gtbeta surface, overlapping the Gtalpha binding surface, explaining how phosducin blocks Gtbetagamma's interaction with Gtalpha. The C-terminal domain shows structural homology to thioredoxin and binds the outer strands of Gtbeta's seventh and first blades in a manner likely to disrupt Gtbetagamma's normal orientation relative to the membrane and receptor. Phosducin's Ser-73, which when phosphorylated inhibits phosducin's function, points away from Gtbetagamma, toward a large flexible loop. Thus phosphorylation is not likely to affect the interface directly, but rather indirectly through an induced conformational change.

PubMed: 8898209
DOI: 10.1016/S0092-8674(00)81376-8

実験手法

X-RAY DIFFRACTION (2.4 Å)