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• W2045803310 endingPage "3658" @default.
• W2045803310 startingPage "3646" @default.
• W2045803310 abstract "Transmembrane (TM) helix-helix interactions are important for virus budding and fusion. We have developed a simulation strategy that reveals the main features of the helical packing between the TM domains of the two glycoproteins E1 and E2 of the α-virus Semliki Forest virus and that can be extrapolated to sketch TM helical packing in other α-viruses. Molecular dynamics simulations were performed in wild-type and mutant peptides, both isolated and forming E1/E2 complexes. The simulations revealed that the isolated wild-type E1 peptide formed a more flexible helix than the rest of peptides and that the wild-type E1/E2 complex consists of two helices that intimately pack their N-terminals. The residues located at the interhelical interface displayed the typical motif of the left-handed coiled-coils. These were small and medium residues as Gly, Ala, Ser, and Leu, which also had the possibility to form interhelical Cα-H… O hydrogen bonds. Results from the mutant complexes suggested that correct packing is a compromise between these residues at both E1 and E2 interhelical interfaces. This compromise allowed prediction of E1-E2 contact residues in the TM spanning domain of other alphaviruses even though the sequence identity of E2 peptides is low in this domain." @default.
• W2045803310 created "2016-06-24" @default.
• W2045803310 creator A5033021345 @default.
• W2045803310 creator A5036730487 @default.
• W2045803310 date "2003-12-01" @default.
• W2045803310 modified "2023-10-03" @default.
• W2045803310 title "Molecular Dynamics Simulations of the E1/E2 Transmembrane Domain of the Semliki Forest Virus" @default.
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• W2045803310 doi "https://doi.org/10.1016/s0006-3495(03)74782-1" @default.
• W2045803310 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1303669" @default.
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• W2045803310 hasPublicationYear "2003" @default.
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