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Atomic structure of the ectodomain from HIV-1 gp41

Author

Listed:
  • W. Weissenhorn

    (The Children's Hospital
    The Children's Hospital)

  • A. Dessen

    (The Children's Hospital)

  • S. C. Harrison

    (The Children's Hospital
    The Children's Hospital
    Howard Hughes Medical Institute, Harvard University)

  • J. J. Skehel

    (National Institute of Medical Research)

  • D. C. Wiley

    (The Children's Hospital
    The Children's Hospital
    Howard Hughes Medical Institute, Harvard University)

Abstract

Fusion of viral and cellular membranes by the envelope glyco-protein gp120/gp41 effects entry of HIV-1 into the cell. The precursor, gp160, is cleaved post-translationally into gp120 and gp41 (refs 1,2), which remain non-covalently associated. Binding to both CD4 and a co-receptor leads to the conformational changes in gp120/gp41 needed for membrane fusion3. We used X-ray crystallography to determine the structure of the protease-resistant part4,5 of a gp41 ectodomain solubilized with a trimeric GCN4 coiled coil in place of the amino-terminal fusion peptide6. The core of the molecule is found to be an extended, triple-stranded a-helical coiled coil with the amino terminus at its tip. A carboxy-terminal α-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 (ref. 7) and in the transmembrane subunit of Moloney murine leukaemia virus8 (Fig. la–d), suggest a common mechanism for initiating fusion.

Suggested Citation

  • W. Weissenhorn & A. Dessen & S. C. Harrison & J. J. Skehel & D. C. Wiley, 1997. "Atomic structure of the ectodomain from HIV-1 gp41," Nature, Nature, vol. 387(6631), pages 426-430, May.
  • Handle: RePEc:nat:nature:v:387:y:1997:i:6631:d:10.1038_387426a0
    DOI: 10.1038/387426a0
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    Cited by:

    1. Javier Guenaga & Richard T Wyatt, 2012. "Structure-guided Alterations of the gp41-directed HIV-1 Broadly Neutralizing Antibody 2F5 Reveal New Properties Regarding its Neutralizing Function," PLOS Pathogens, Public Library of Science, vol. 8(7), pages 1-15, July.
    2. Gregory H. Bird & J. J. Patten & William Zavadoski & Nicole Barucci & Marina Godes & Benjamin M. Moyer & Callum D. Owen & Paul DaSilva-Jardine & Donna S. Neuberg & Richard A. Bowen & Robert A. Davey &, 2024. "A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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