Retrovirus envelope domain at 1.7 angstrom resolution.
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 MoMuLV TM 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.
Fass
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Howard Hughes Medical Institute, Cambridge, Massachusetts, 02142, USA.
Harrison
S C
SC
Kim
P S
PS
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008979:Moloney murine leukemia virus / Q000737:chemistry* / Q000254:growth & development; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D012191:Retroviridae Proteins / Q000737:chemistry*; D014759:Viral Envelope Proteins / Q000737:chemistry*
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D010446:Peptide Fragments; D012191:Retroviridae Proteins; D014759:Viral Envelope Proteins