5JYN

Structure of the transmembrane domain of HIV-1 gp41 in bicelle

5JYN の概要

• エントリーDOI: 10.2210/pdb5jyn/pdb
• NMR情報: BMRB: 30090
• 分子名称: Envelope glycoprotein gp160 (1 entity in total)
• 機能のキーワード: transmembrane domain, lipid bilayer, transmembrane trimer, viral protein
• 由来する生物種: Human immunodeficiency virus 1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 13951.81

構造登録者

Dev, J.,Fu, Q.,Park, D.,Chen, B.,Chou, J.J. (登録日: 2016-05-14, 公開日: 2016-06-29, 最終更新日: 2024-05-15)

主引用文献

Dev, J.,Park, D.,Fu, Q.,Chen, J.,Ha, H.J.,Ghantous, F.,Herrmann, T.,Chang, W.,Liu, Z.,Frey, G.,Seaman, M.S.,Chen, B.,Chou, J.J.
Structural basis for membrane anchoring of HIV-1 envelope spike.
Science, 353:172-175, 2016

PubMed Abstract: HIV-1 envelope spike (Env) is a type I membrane protein that mediates viral entry. We used nuclear magnetic resonance to determine an atomic structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in bicelles that mimic a lipid bilayer. The TM forms a well-ordered trimer that protects a conserved membrane-embedded arginine. An amino-terminal coiled-coil and a carboxyl-terminal hydrophilic core stabilize the trimer. Individual mutations of conserved residues did not disrupt the TM trimer and minimally affected membrane fusion and infectivity. Major changes in the hydrophilic core, however, altered the antibody sensitivity of Env. These results show how a TM domain anchors, stabilizes, and modulates a viral envelope spike and suggest that its influence on Env conformation is an important consideration for HIV-1 immunogen design.

PubMed: 27338706
DOI: 10.1126/science.aaf7066

実験手法

SOLUTION NMR