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| Home > Publications database > Full length Vpu from HIV-1: Combining molecular dynamics simulations with NMR spectroscopy |
| Journal Article | PreJuSER-55021 |
; ; ; ;
2006
Adenine Press
Guilderland, NY
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Abstract: Based on structures made available by solution NMR, molecular models of the protein Vpu from HIV-1 were built and refined by 6 ns MD simulations in a fully hydrated lipid bilayer. Vpu is an 81 amino acid type I integral membrane protein encoded by the human immunodeficiency virus type-1 (HIV- 1) and closely related simian immunodeficiency viruses (SIVs). Its role is to amplify viral release. Upon phosphorylation, the cytoplasmic domain adopts a more compact shape with helices 2 and 3 becoming almost parallel to each other. A loss of helicity for several residues belonging to the helices adjacent to both ends of the loop region containing serines 53 and 57 is observed. A fourth helix, present in one of: the NMR-based Structures of the cytoplasmic domain and located near the C-terminus, is lost upon phosphorylation.
Keyword(s): J ; Vpu (auto) ; HIV-1 (auto) ; membrane protein (auto) ; molecular dynamics simulations (auto) ; NMR spectroscopy (auto)
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