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000006550 0247_ $$2DOI$$a10.1111/j.1742-4658.2009.07363.x
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000006550 084__ $$2WoS$$aBiochemistry & Molecular Biology
000006550 1001_ $$0P:(DE-Juel1)VDB28257$$aWittlich, M.$$b0$$uFZJ
000006550 245__ $$aNMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles
000006550 260__ $$aOxford [u.a.]$$bWiley-Blackwell$$c2009
000006550 300__ $$a6560 - 6575
000006550 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000006550 440_0 $$017341$$aFEBS Journal$$v276$$x1742-464X$$y22
000006550 500__ $$aThis work was supported by a grant from the Prasidentenfond der Helmholtzgemeinschaft (HGF, Virtual Institute of Structural Biology) to DW.
000006550 520__ $$aThe HIV-1 encoded virus protein U (VpU) is required for efficient viral release from human host cells and for induction of CD4 degradation in the endoplasmic reticulum. The cytoplasmic domain of the membrane protein VpU (VpUcyt) is essential for the latter activity. The structure and dynamics of VpUcyt were characterized in the presence of membrane simulating dodecylphosphatidylcholine (DPC) micelles by high-resolution liquid state NMR. VpUcyt is unstructured in aqueous buffer. The addition of DPC micelles induces a well-defined membrane proximal alpha-helix (residues I39-E48) and an additional helical segment (residues L64-R70). A tight loop (L73-V78) is observed close to the C-terminus, whereas the interhelical linker (R49-E63) remains highly flexible. A 3D structure of VpUcyt in the presence of DPC micelles was calculated from a large set of proton-proton distance constraints. The topology of micelle-associated VpUcyt was derived from paramagnetic relaxation enhancement of protein nuclear spins after the introduction of paramagnetic probes into the interior of the micelle or the aqueous buffer. Qualitative analysis of secondary chemical shift and paramagnetic relaxation enhancement data in conjunction with dynamic information from heteronuclear NOEs and structural insight from homonuclear NOE-based distance constraints indicated that micelle-associated VpUcyt retains a substantial degree of structural flexibility.
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000006550 650_2 $$2MeSH$$aHIV-1: chemistry
000006550 650_2 $$2MeSH$$aHIV-1: metabolism
000006550 650_2 $$2MeSH$$aHuman Immunodeficiency Virus Proteins: chemistry
000006550 650_2 $$2MeSH$$aMagnetic Resonance Spectroscopy
000006550 650_2 $$2MeSH$$aMicelles
000006550 650_2 $$2MeSH$$aPhosphorylcholine: analogs & derivatives
000006550 650_2 $$2MeSH$$aPhosphorylcholine: chemistry
000006550 650_2 $$2MeSH$$aProtein Structure, Tertiary
000006550 650_2 $$2MeSH$$aViral Regulatory and Accessory Proteins: chemistry
000006550 650_7 $$00$$2NLM Chemicals$$aHuman Immunodeficiency Virus Proteins
000006550 650_7 $$00$$2NLM Chemicals$$aMicelles
000006550 650_7 $$00$$2NLM Chemicals$$aViral Regulatory and Accessory Proteins
000006550 650_7 $$00$$2NLM Chemicals$$avpu protein, Human immunodeficiency virus 1
000006550 650_7 $$0107-73-3$$2NLM Chemicals$$aPhosphorylcholine
000006550 650_7 $$053949-18-1$$2NLM Chemicals$$adodecylphosphocholine
000006550 650_7 $$2WoSType$$aJ
000006550 65320 $$2Author$$aCD4
000006550 65320 $$2Author$$aDPC micelle
000006550 65320 $$2Author$$aHIV-1 VpU
000006550 65320 $$2Author$$aNMR
000006550 65320 $$2Author$$asolution structure
000006550 7001_ $$0P:(DE-Juel1)132009$$aKoenig, B. W.$$b1$$uFZJ
000006550 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b2$$uFZJ
000006550 7001_ $$0P:(DE-HGF)0$$aSchmidt, H.$$b3
000006550 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000006550 773__ $$0PERI:(DE-600)2172518-4$$a10.1111/j.1742-4658.2009.07363.x$$gVol. 276, p. 6560 - 6575$$p6560 - 6575$$q276<6560 - 6575$$tThe @FEBS journal$$v276$$x1742-464X$$y2009
000006550 8567_ $$uhttp://dx.doi.org/10.1111/j.1742-4658.2009.07363.x
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000006550 9141_ $$y2009
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