8P13

Cryo-EM structure of Rhodopsin-Gi bound with antibody fragments scFv16 and Fab79, conformation 1

これはPDB形式変換不可エントリーです。

8P13 の概要

• エントリーDOI: 10.2210/pdb8p13/pdb
• EMDBエントリー: 17343 17344 17345
• 分子名称: Rhodopsin, Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (7 entities in total)
• 機能のキーワード: gpcr, rhodopsin, g protein, fab, signaling protein
• 由来する生物種: Bos taurus (cattle); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 210325.90

構造登録者

Pamula, F.,Tejero, O.,Muehle, J.,Thoma, R.,Schertler, G.F.X.,Marino, J.,Tsai, C.-J. (登録日: 2023-05-11, 公開日: 2024-11-20, 最終更新日: 2025-10-29)

主引用文献

Pamula, F.,Tejero, O.,Muhle, J.,Thoma, R.,Schertler, G.F.X.,Marino, J.,Tsai, C.J.
Tool antibody fragments reveal multiple conformations of the rhodopsin-Gi signaling complex.
Biophys.J., 2025

PubMed Abstract: Antibody Fab fragments are widely used protein binders that assist in structural studies of G-protein-coupled receptor (GPCR) signaling complexes. Expanding the repertoire of such binders to target distinct components of the signaling complex offers opportunities to probe conformational regulation and dynamics. Here, we report the biochemical and cryo-EM characterization of two Fab fragments, Fab79 and Fab13, raised against the rhodopsin-Gαiβγ complex. Fab79 binds to the flexible α-helical domain (AHD) of the Gαi subunit and prevents complex dissociation in the presence of the nonhydrolyzable GTP analog, GTPγS, likely by hindering AHD closure, a step necessary for complex dissociation. In contrast, Fab13 binds rigidly to Gβ without directly contacting Gα or the receptor. These findings show that Fab79 and Fab13 reveal functionally relevant conformational states of G-protein activation and serve as practical tools to stabilize or modulate GPCR signaling complexes.

PubMed: 41029899
DOI: 10.1016/j.bpj.2025.09.044

実験手法

ELECTRON MICROSCOPY (5.2 Å)