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.
Original language | English |
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Pages (from-to) | 485-496 |
Number of pages | 12 |
Journal | Journal of Biomolecular Structure and Dynamics |
Volume | 23 |
Issue number | 5 |
DOIs | |
State | Published - Apr 2006 |
Keywords
- HIV-1
- Membrane protein
- Molecular dynamics simulations
- NMR spectroscopy
- Vpu