Atomic structure of the ectodomain from HIV-1 gp41

W. Weissenhorn, A. Dessen, S. C. Harrison, J. J. Skehel and D. C. Wiley
Additional contact information
W. Weissenhorn: The Children's Hospital
A. Dessen: The Children's Hospital
S. C. Harrison: The Children's Hospital
J. J. Skehel: National Institute of Medical Research
D. C. Wiley: The Children's Hospital

Nature, 1997, vol. 387, issue 6631, 426-430

Abstract: 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.

Date: 1997
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/387426a0 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:387:y:1997:i:6631:d:10.1038_387426a0

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/387426a0

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().