1AGR

COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4

1AGR の概要

• エントリーDOI: 10.2210/pdb1agr/pdb
• 分子名称: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I), RGS4, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: gi-alpha-1, hydrolase, signal transduction, rgs4, complex (signal transduction-regulator), gtp-binding, gtpase activating protein, complex (signal transduction-regulator) complex, complex (signal transduction/regulator)
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Nucleus: P10824
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 128634.28

構造登録者

Tesmer, J.J.G.,Sprang, S.R. (登録日: 1997-03-25, 公開日: 1997-06-16, 最終更新日: 2024-05-22)

主引用文献

Tesmer, J.J.,Berman, D.M.,Gilman, A.G.,Sprang, S.R.
Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis.
Cell(Cambridge,Mass.), 89:251-261, 1997

PubMed Abstract: RGS proteins are GTPase activators for heterotrimeric G proteins. We report here the 2.8 A resolution crystal structure of the RGS protein RGS4 complexed with G(i alpha1)-Mg2+-GDP-AlF4 . Only the core domain of RGS4 is visible in the crystal. The core domain binds to the three switch regions of G(i alpha1), but does not contribute catalytic residues that directly interact with either GDP or AlF4-. Therefore, RGS4 appears to catalyze rapid hydrolysis of GTP primarily by stabilizing the switch regions of G(i alpha1), although the conserved Asn-128 from RGS4 could also play a catalytic role by interacting with the hydrolytic water molecule or the side chain of Gln-204. The binding site for RGS4 on G(i alpha1) is also consistent with the activity of RGS proteins as antagonists of G(alpha) effectors.

PubMed: 9108480
DOI: 10.1016/S0092-8674(00)80204-4

実験手法

X-RAY DIFFRACTION (2.8 Å)