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PDBsum entry 1env
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Viral protein
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PDB id
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1env
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Atomic structure of the ectodomain from HIV-1 gp41.
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Authors
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W.Weissenhorn,
A.Dessen,
S.C.Harrison,
J.J.Skehel,
D.C.Wiley.
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Ref.
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Nature, 1997,
387,
426-430.
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PubMed id
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Abstract
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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.
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