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• W2171542740 startingPage "1281" @default.
• W2171542740 abstract "The envelope (Env) protein of Moloney murine leukemia virus (MoMuLV) is a homotrimeric complex whose monomers consist of linked surface (SU) and transmembrane (TM) proteins cleaved from a precursor protein by a cellular protease. In addition, a significant fraction of virion-associated TM is further processed by the viral protease to remove the C-terminal 16 amino acids of the cytoplasmic domain, the R peptide. This cleavage greatly enhances the fusogenicity of the protein and is necessary for the formation of a fully functional Env protein complex. We have previously proposed that R peptide cleavage enhances fusogenicity by altering the conformation of the ectodomain of the protein (Y. Zhao et al., J. Virol. 72:5392-5398, 1998). Using a series of truncation and point mutants of MoMuLV Env, we now provide direct biochemical and immunological evidence that the cytoplasmic tail and the membrane-spanning region of Env can influence the overall structure of the ectodomain of the protein and alter the strength of the SU-TM interaction. The R-peptide-truncated form of the protein, in particular, exhibits a markedly different conformation than the full-length protein." @default.
• W2171542740 created "2016-06-24" @default.
• W2171542740 creator A5032868413 @default.
• W2171542740 creator A5085998035 @default.
• W2171542740 creator A5089860825 @default.
• W2171542740 date "2003-01-15" @default.
• W2171542740 modified "2023-09-25" @default.
• W2171542740 title "Cytoplasmic Tail of Moloney Murine Leukemia Virus Envelope Protein Influences the Conformation of the Extracellular Domain: Implications for Mechanism of Action of the R Peptide" @default.
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• W2171542740 doi "https://doi.org/10.1128/jvi.77.2.1281-1291.2003" @default.
• W2171542740 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/140788" @default.
• W2171542740 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12502845" @default.
• W2171542740 hasPublicationYear "2003" @default.
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