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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.

Original publication

DOI

10.1080/07391102.2006.10507074

Type

Journal article

Journal

J Biomol Struct Dyn

Publication Date

04/2006

Volume

23

Pages

485 - 496

Keywords

Amino Acid Sequence, Binding Sites, Computer Simulation, HIV-1, Human Immunodeficiency Virus Proteins, Humans, Lipid Bilayers, Magnetic Resonance Spectroscopy, Membrane Lipids, Models, Molecular, Molecular Sequence Data, Phosphorylation, Protein Conformation, Protein Folding, Viral Regulatory and Accessory Proteins, Water