Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 23, Issue 5, Pages 485-496Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2006.10507074
Keywords
Vpu; HIV-1; membrane protein; molecular dynamics simulations; NMR spectroscopy
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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.
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