4G5O

Structure of LGN GL4/Galphai3(Q147L) complex

4G5O の概要

• エントリーDOI: 10.2210/pdb4g5o/pdb
• 関連するPDBエントリー: 4G5Q 4G5R 4G5S
• 分子名称: Guanine nucleotide-binding protein G(k) subunit alpha, G-protein-signaling modulator 2, GUANOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: galphai, goloco, galpha signaling, asymmetric cell division, cell cycle-signaling protein complex, cell cycle/signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P08754; Cytoplasm (By similarity): Q8VDU0
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 168585.12

構造登録者

Jia, M.,Li, J.,Zhu, J.,Wen, W.,Zhang, M.,Wang, W. (登録日: 2012-07-18, 公開日: 2012-09-05, 最終更新日: 2025-03-05)

主引用文献

Jia, M.,Li, J.,Zhu, J.,Wen, W.,Zhang, M.,Wang, W.
Crystal structures of the scaffolding protein LGN reveal the general mechanism by which GoLoco binding motifs inhibit the release of GDP from G alpha i.
J.Biol.Chem., 287:36766-36776, 2012

PubMed Abstract: GoLoco (GL) motif-containing proteins regulate G protein signaling by binding to Gα subunit and acting as guanine nucleotide dissociation inhibitors. GLs of LGN are also known to bind the GDP form of Gα(i/o) during asymmetric cell division. Here, we show that the C-terminal GL domain of LGN binds four molecules of Gα(i)·GDP. The crystal structures of Gα(i)·GDP in complex with LGN GL3 and GL4, respectively, reveal distinct GL/Gα(i) interaction features when compared with the only high resolution structure known with GL/Gα(i) interaction between RGS14 and Gα(i1.) Only a few residues C-terminal to the conserved GL sequence are required for LGN GLs to bind to Gα(i)·GDP. A highly conserved "double Arg finger" sequence (RΨ(D/E)(D/E)QR) is responsible for LGN GL to bind to GDP bound to Gα(i). Together with the sequence alignment, we suggest that the LGN GL/Gα(i) interaction represents a general binding mode between GL motifs and Gα(i). We also show that LGN GLs are potent guanine nucleotide dissociation inhibitors.

PubMed: 22952234
DOI: 10.1074/jbc.M112.391607

実験手法

X-RAY DIFFRACTION (2.9 Å)