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@ARTICLE{Wittlich:6550,
author = {Wittlich, M. and Koenig, B. W. and Stoldt, M. and Schmidt,
H. and Willbold, D.},
title = {{NMR} structural characterization of {HIV}-1 virus protein
{U} cytoplasmic domain in the presence of
dodecylphosphatidylcholine micelles},
journal = {The FEBS journal},
volume = {276},
issn = {1742-464X},
address = {Oxford [u.a.]},
publisher = {Wiley-Blackwell},
reportid = {PreJuSER-6550},
pages = {6560 - 6575},
year = {2009},
note = {This work was supported by a grant from the Prasidentenfond
der Helmholtzgemeinschaft (HGF, Virtual Institute of
Structural Biology) to DW.},
abstract = {The HIV-1 encoded virus protein U (VpU) is required for
efficient viral release from human host cells and for
induction of CD4 degradation in the endoplasmic reticulum.
The cytoplasmic domain of the membrane protein VpU (VpUcyt)
is essential for the latter activity. The structure and
dynamics of VpUcyt were characterized in the presence of
membrane simulating dodecylphosphatidylcholine (DPC)
micelles by high-resolution liquid state NMR. VpUcyt is
unstructured in aqueous buffer. The addition of DPC micelles
induces a well-defined membrane proximal alpha-helix
(residues I39-E48) and an additional helical segment
(residues L64-R70). A tight loop (L73-V78) is observed close
to the C-terminus, whereas the interhelical linker (R49-E63)
remains highly flexible. A 3D structure of VpUcyt in the
presence of DPC micelles was calculated from a large set of
proton-proton distance constraints. The topology of
micelle-associated VpUcyt was derived from paramagnetic
relaxation enhancement of protein nuclear spins after the
introduction of paramagnetic probes into the interior of the
micelle or the aqueous buffer. Qualitative analysis of
secondary chemical shift and paramagnetic relaxation
enhancement data in conjunction with dynamic information
from heteronuclear NOEs and structural insight from
homonuclear NOE-based distance constraints indicated that
micelle-associated VpUcyt retains a substantial degree of
structural flexibility.},
keywords = {HIV-1: chemistry / HIV-1: metabolism / Human
Immunodeficiency Virus Proteins: chemistry / Magnetic
Resonance Spectroscopy / Micelles / Phosphorylcholine:
analogs $\&$ derivatives / Phosphorylcholine: chemistry /
Protein Structure, Tertiary / Viral Regulatory and Accessory
Proteins: chemistry / Human Immunodeficiency Virus Proteins
(NLM Chemicals) / Micelles (NLM Chemicals) / Viral
Regulatory and Accessory Proteins (NLM Chemicals) / vpu
protein, Human immunodeficiency virus 1 (NLM Chemicals) /
Phosphorylcholine (NLM Chemicals) / dodecylphosphocholine
(NLM Chemicals) / J (WoSType)},
cin = {ISB-3},
ddc = {540},
cid = {I:(DE-Juel1)VDB942},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:19804408},
UT = {WOS:000271057200015},
doi = {10.1111/j.1742-4658.2009.07363.x},
url = {https://juser.fz-juelich.de/record/6550},
}