3CX8

Crystal Structure of PDZRhoGEF rgRGS Domain in a Complex with Galpha-13 Bound to GTP-gamma-S

3CX8 の概要

• エントリーDOI: 10.2210/pdb3cx8/pdb
• 関連するPDBエントリー: 1SHZ 3CX6 3CX7
• 分子名称: Guanine nucleotide-binding protein alpha-13 subunit, Rho guanine nucleotide exchange factor 11, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: signal transduction, protein complex, gtp-binding, lipoprotein, membrane, nucleotide-binding, palmitate, phosphoprotein, transducer, coiled coil, cytoplasm, gtpase activation, guanine-nucleotide releasing factor, signaling protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Membrane ; Lipid-anchor : P27601; Cytoplasm : Q9ES67
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63630.42

構造登録者

Sprang, S.R.,Chen, Z. (登録日: 2008-04-23, 公開日: 2008-10-28, 最終更新日: 2023-08-30)

主引用文献

Chen, Z.,Singer, W.D.,Danesh, S.M.,Sternweis, P.C.,Sprang, S.R.
Recognition of the Activated States of Galpha13 by the rgRGS Domain of PDZRhoGEF.
Structure, 16:1532-1543, 2008

PubMed Abstract: G12 class heterotrimeric G proteins stimulate RhoA activation by RGS-RhoGEFs. However, p115RhoGEF is a GTPase Activating Protein (GAP) toward Galpha13, whereas PDZRhoGEF is not. We have characterized the interaction between the PDZRhoGEF rgRGS domain (PRG-rgRGS) and the alpha subunit of G13 and have determined crystal structures of their complexes in both the inactive state bound to GDP and the active states bound to GDP*AlF (transition state) and GTPgammaS (Michaelis complex). PRG-rgRGS interacts extensively with the helical domain and the effector-binding sites on Galpha13 through contacts that are largely conserved in all three nucleotide-bound states, although PRG-rgRGS has highest affinity to the Michaelis complex. An acidic motif in the N terminus of PRG-rgRGS occupies the GAP binding site of Galpha13 and is flexible in the GDP*AlF complex but well ordered in the GTPgammaS complex. Replacement of key residues in this motif with their counterparts in p115RhoGEF confers GAP activity.

PubMed: 18940608
DOI: 10.1016/j.str.2008.07.009

実験手法

X-RAY DIFFRACTION (2 Å)