Nature Structural Biology
3, 465 - 469 (1996)
doi:10.1038/nsb0596-465
Retrovirus envelope domain at 1.7 Å resolutionDeborah Fass1, Stephen C. Harrison2
& Peter S. Kim1
1 Howard Hughes Medical Institute Whitehead Institute for Biomedical Research Department of Biology Massachusetts Institute of Technology Nine Cambridge Center, Cambridge, Massachusetts, 02142 USA
2Howard Hughes Medical Institute Department of Molecular and Cellular Biology Harvard University 7 Divinity Avenue, Cambridge, Massachusetts, 02138 USA We report the crystal structure of an extraviral segment of a retrovirus envelope protein, the Moloney murine leukemia virus (MoMuLV) transmembrane (TM) subunit. This segment, which comprises a region of the MoMuLVTM protein analogous to that contained within the X-ray crystal structure of low-pH converted influenza hemagglutinin, contains a trimeric coiled coil, with a hydrophobic cluster at its base and a strand that packs in an antiparallel orientation against the coiled coil. This structure gives the first high-resolution insight into the retrovirus surface and serves as a model for a wide range of viral fusion proteins; key residues in this structure are conserved among C- and D-type retroviruses and the filovirus ebola.
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