TY  - JOUR
AU  - Lemaitre, V.
AU  - Wray, V.
AU  - Willbold, D.
AU  - Watts, A.
AU  - Fischer, W. B.
TI  - Full length Vpu from HIV-1: Combining molecular dynamics simulations with NMR spectroscopy
JO  - Journal of biomolecular structure & dynamics
VL  - 23
SN  - 0739-1102
CY  - Guilderland, NY
PB  - Adenine Press
M1  - PreJuSER-55021
SP  - 485 - 496
PY  - 2006
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000236290300001
UR  - https://juser.fz-juelich.de/record/55021
ER  -