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1DF5

INTERACTIONS BETWEEN HIV-1 GP41 CORE AND DETERGENTS AND THEIR IMPLICATIONS FOR MEMBRANE FUSION

1DF5 の概要
エントリーDOI10.2210/pdb1df5/pdb
関連するPDBエントリー1DF4
分子名称HIV-1 ENVELOPE GLYCOPROTEIN GP41 (1 entity in total)
機能のキーワードhiv-1, gp41, membrane fusion, protein-detergent interaction, viral protein
由来する生物種Human immunodeficiency virus 1
詳細
細胞内の位置Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P04578
タンパク質・核酸の鎖数1
化学式量合計7879.75
構造登録者
Shu, W.,Ji, H.,Lu, M. (登録日: 1999-11-17, 公開日: 1999-11-24, 最終更新日: 2024-02-07)
主引用文献Shu, W.,Ji, H.,Lu, M.
Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion.
J.Biol.Chem., 275:1839-1845, 2000
Cited by
PubMed Abstract: The gp41 envelope protein mediates entry of human immunodeficiency virus type 1 (HIV-1) into the cell by promoting membrane fusion. The crystal structure of a gp41 ectodomain core in its fusion-active state is a six-helix bundle in which a N-terminal trimeric coiled coil is surrounded by three C-terminal outer helices in an antiparallel orientation. Here we demonstrate that the N34(L6)C28 model of the gp41 core is stabilized by interaction with the ionic detergent sodium dodecyl sulfate (SDS) or the nonionic detergent n-octyl-beta-D-glucopyranoside (betaOG). The high resolution x-ray structures of N34(L6)C28 crystallized from two different detergent micellar media reveal a six-helix bundle conformation very similar to that of the molecule in water. Moreover, N34(L6)C28 adopts a highly alpha-helical conformation in lipid vesicles. Taken together, these results suggest that the six-helix bundle of the gp41 core displays substantial affinity for lipid bilayers rather than unfolding in the membrane environment. This characteristic may be important for formation of the fusion-active gp41 core structure and close apposition of the viral and cellular membranes for fusion.
PubMed: 10636883
DOI: 10.1074/jbc.275.3.1839
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 1df5
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-03-04に公開中

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