%0 Journal Article
%A Lemaitre, V.
%A Wray, V.
%A Willbold, D.
%A Watts, A.
%A Fischer, W. B.
%T Full length Vpu from HIV-1: Combining molecular dynamics simulations with NMR spectroscopy
%J Journal of biomolecular structure & dynamics
%V 23
%@ 0739-1102
%C Guilderland, NY
%I Adenine Press
%M PreJuSER-55021
%P 485 - 496
%D 2006
%Z Record converted from VDB: 12.11.2012
%X 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.
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000236290300001
%U https://juser.fz-juelich.de/record/55021