1ENV

ATOMIC STRUCTURE OF THE ECTODOMAIN FROM HIV-1 GP41

1ENV の概要

• エントリーDOI: 10.2210/pdb1env/pdb
• 分子名称: HIV-1 ENVELOPE PROTEIN CHIMERA CONSISTING OF A FRAGMENT OF GCN4 ZIPPER CLONED N-TERMINAL TO TWO FRAGMENTS OF GP41 (2 entities in total)
• 機能のキーワード: viral fusion, coat protein, viral protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 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: P03377
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14709.76

構造登録者

Weissenhorn, W.,Dessen, A.,Harrison, S.C.,Skehel, J.J.,Wiley, D.C. (登録日: 1997-06-27, 公開日: 1997-11-19, 最終更新日: 2024-02-07)

主引用文献

Weissenhorn, W.,Dessen, A.,Harrison, S.C.,Skehel, J.J.,Wiley, D.C.
Atomic structure of the ectodomain from HIV-1 gp41.
Nature, 387:426-430, 1997

PubMed Abstract: Fusion of viral and cellular membranes by the envelope glycoprotein gp120/gp41 effects entry of HIV-1 into the cell. The precursor, gp160, is cleaved post-translationally into gp120 and gp41 which remain non-covalently associated. Binding to both CD4 and a co-receptor leads to the conformational changes in gp120/gp41 needed for membrane fusion. We used X-ray crystallography to determine the structure of the protease-resistant part of a gp41 ectodomain solubilized with a trimeric GCN4 coiled coil in place of the amino-terminal fusion peptide. The core of the molecule is found to be an extended, triple-stranded alpha-helical coiled coil with the amino terminus at its tip. A carboxy-terminal alpha-helix packs in the reverse direction against the outside of the coiled coil, placing the amino and carboxy termini near each other at one end of the long rod. These features, and the existence of a similar reversal of chain direction in the fusion pH-induced conformation of influenza virus HA2 and in the transmembrane subunit of Moloney murine leukaemia virus (Fig. 1a-d), suggest a common mechanism for initiating fusion.

PubMed: 9163431
DOI: 10.1038/387426a0

実験手法

X-RAY DIFFRACTION (2.6 Å)