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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},
}