5VVF

Crystal Structure of 354BG1 Fab

5VVF の概要

• エントリーDOI: 10.2210/pdb5vvf/pdb
• 分子名称: 354BG1 Heavy Chain, 354BG1 Light Chain, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: hiv, broadly neutralizing antibody, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50700.50

構造登録者

Scharf, L.,Gristick, H.B.,Bjorkman, P.J. (登録日: 2017-05-19, 公開日: 2017-12-06, 最終更新日: 2024-11-06)

主引用文献

Wang, H.,Gristick, H.B.,Scharf, L.,West, A.P.,Galimidi, R.P.,Seaman, M.S.,Freund, N.T.,Nussenzweig, M.C.,Bjorkman, P.J.
Asymmetric recognition of HIV-1 Envelope trimer by V1V2 loop-targeting antibodies.
Elife, 6:-, 2017

PubMed Abstract: The HIV-1 envelope (Env) glycoprotein binds to host cell receptors to mediate membrane fusion. The prefusion Env trimer is stabilized by V1V2 loops that interact at the trimer apex. Broadly neutralizing antibodies (bNAbs) against V1V2 loops, exemplified by PG9, bind asymmetrically as a single Fab to the apex of the symmetric Env trimer using a protruding CDRH3 to penetrate the Env glycan shield. Here we characterized a distinct mode of V1V2 epitope recognition by the new bNAb BG1 in which two Fabs bind asymmetrically per Env trimer using a compact CDRH3. Comparisons between cryo-EM structures of Env trimer complexed with BG1 (6.2 Å resolution) and PG9 (11.5 Å resolution) revealed a new V1V2-targeting strategy by BG1. Analyses of the EM structures provided information relevant to vaccine design including molecular details for different modes of asymmetric recognition of Env trimer and a binding model for BG1 recognition of V1V2 involving glycan flexibility.

PubMed: 28548638
DOI: 10.7554/eLife.27389

実験手法

X-RAY DIFFRACTION (2 Å)