3Q85

Crystal Structure of Rem2 G-domain -GTP Analog Complex

3Q85 の概要

• エントリーDOI: 10.2210/pdb3q85/pdb
• 関連するPDBエントリー: 2DPX 3CBQ 3Q72 3Q7P 3Q7Q
• 分子名称: GTP-binding protein REM 2, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: g-domain, g-protein, cav2 beta, signaling protein
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cell membrane (By similarity): Q8VEL9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39102.01

構造登録者

Navon-Perry, L.,Hirsch, J.A. (登録日: 2011-01-06, 公開日: 2011-09-21, 最終更新日: 2023-09-13)

主引用文献

Sasson, Y.,Navon-Perry, L.,Huppert, D.,Hirsch, J.A.
RGK Family G-Domain:GTP Analog Complex Structures and Nucleotide-Binding Properties.
J.Mol.Biol., 413:372-389, 2011

PubMed Abstract: The RGK family of small G-proteins, including Rad, Gem, Rem1, and Rem2, is inducibly expressed in various mammalian tissues and interacts with voltage-dependent calcium channels and Rho kinase. Many questions remain regarding their physiological roles and molecular mechanism. Previous crystallographic studies reported RGK G-domain:guanosine di-phosphate structures. To test whether RGK proteins undergo a nucleotide-induced conformational change, we determined the crystallographic structures of Rad:GppNHp and Rem2:GppNHp to 1.7 and 1.8 Å resolutions, respectively. Also, we characterized the nucleotide-binding properties and conformations for Gem, Rad, and several structure-based mutants using fluorescence spectroscopy. The results suggest that RGK G-proteins may not behave as Ras-like canonical nucleotide-induced molecular switches. Further, the RGK proteins have differing structures and nucleotide-binding properties, which may have implications for their varied action on effectors.

PubMed: 21903096
DOI: 10.1016/j.jmb.2011.08.017

実験手法

X-RAY DIFFRACTION (1.757 Å)