TAILIEUCHUNG - Báo cáo khoa học: NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles

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 dynam-ics of VpUcyt were characterized in the presence of membrane simulating dodecylphosphatidylcholine (DPC) micelles by high-resolution liquid state NMR. | ễFEBS Journal NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles Marc Wittlich1 2 Bernd W. Koenig1 2 Matthias Stoldt1 2 Holger Schmidt1 2 and Dieter Willbold1 2 1 Institut fur Strukturbiologie und Biophysik ISB-3 Forschungszentrum Jijlich Germany 2 Institut fur Physikalische Biologie Heinrich-Heine-Universitat Dusseldorf Germany Keywords CD4 DPC micelle HIV-1 VpU NMR solution structure Correspondence D. Willbold Forschungszentrum Julich GmbH ISB-3 52425 Julich Germany Fax 49 2461612023 Tel 49 2461612100 E-mail Present address Max-Planck-Institute for Biophysical Chemistry NMR-based StructuralBiology Gottingen Germany Database Resonance assignment tables have been deposited at the BiologicalMagnetic Resonance Data Bank BMRB under the accession code 15513 Received 31 May 2009 revised 2 September 2009 accepted 7 September 2009 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 a-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

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