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@ARTICLE{Wittlich:62891,
      author       = {Wittlich, M. and Koenig, B. W. and Willbold, D.},
      title        = {{S}tructural {C}onsequences of {P}hosphorylations of two
                      {S}erine {R}esidues in the {C}ytoplasmic {D}omain of {HIV}-1
                      {V}p{U}},
      journal      = {Journal of peptide science},
      volume       = {14},
      issn         = {1075-2617},
      address      = {New York, NY [u.a.]},
      publisher    = {Wiley},
      reportid     = {PreJuSER-62891},
      pages        = {804 - 810},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The human immunodeficiency virus type 1 (HIV-1) protein U
                      (VpU) is an accessory protein responsible for enhancement of
                      viral particle release and down regulation of the
                      T-lymphocyte coreceptor CD4. Direct binding between the
                      cytoplasmic domains of CD4 and VpU as well as
                      phosphorylation of serines 53 and 57 in the cytoplasmic
                      domain of VpU plays a central role in CD4 downregulation. We
                      investigated structural consequences of phosphorylation of
                      the two serines using nuclear magnetic resonance
                      spectroscopy. A uniformly 15N and 13C stable isotope-labeled
                      45-residue peptide comprising the cytoplasmic domain of VpU
                      (VpUcyt) was recombinantly produced in E .coli. The peptide
                      forms two helices (commonly referred to as helix 2 and 3) in
                      the presence of membrane mimicking dodecylphosphocholine
                      (DPC) micelles, which flank a flexible region containing the
                      two phosphorylation sites. Phosphorylation does not cause
                      any drastic structural changes in the secondary structure of
                      VpUcyt. However, an N-terminal elongation of helix 3 and a
                      slightly reduced helicity at the C-terminus of helix 2 are
                      observed upon phosphorylation based on characteristic
                      changes of 13Calpha and 13Cbeta chemical shifts.
                      Phosphorylation also reduces the local mobility of the
                      protein backbone in the loop region containing the
                      phosphorylation sites according to heteronuclear 1H--15N
                      nuclear Overhauser enhancement (NOE) data.},
      keywords     = {Cytoplasm: chemistry / Cytoplasm: metabolism / HIV-1:
                      chemistry / Human Immunodeficiency Virus Proteins: chemistry
                      / Human Immunodeficiency Virus Proteins: metabolism /
                      Nuclear Magnetic Resonance, Biomolecular / Phosphoserine:
                      chemistry / Phosphoserine: metabolism / Protein Structure,
                      Tertiary / Viral Regulatory and Accessory Proteins:
                      chemistry / Viral Regulatory and Accessory Proteins:
                      metabolism / Human Immunodeficiency Virus Proteins (NLM
                      Chemicals) / Viral Regulatory and Accessory Proteins (NLM
                      Chemicals) / vpu protein, Human immunodeficiency virus 1
                      (NLM Chemicals) / Phosphoserine (NLM Chemicals) / J
                      (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Chemistry,
                      Analytical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18186541},
      UT           = {WOS:000257725000004},
      doi          = {10.1002/psc.1004},
      url          = {https://juser.fz-juelich.de/record/62891},
}