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@ARTICLE{Singh:22825,
      author       = {Singh, S. and Möckel, L. and Thiagarajan-Rosenkranz, P.
                      and Wittlich, M. and Willbold, D. and Koenig, B.},
      title        = {{M}apping the interaction between the cytoplasmic domains
                      of {HIV}-1 {V}p{U} and human {CD}4 using {NMR}
                      spectroscopy.},
      journal      = {The FEBS journal},
      volume       = {279},
      issn         = {1742-464X},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {PreJuSER-22825},
      pages        = {3705 - 3714},
      year         = {2012},
      note         = {S. K. Singh is a collegiate of the Jurgen Manchot graduate
                      school 'Molecules of infection' at the Heinrich Heine
                      University Dusseldorf. This work was supported by a grant
                      from the Prasidentenfond der Helmholtz-Gemeinschaft (HGF,
                      'Virtual Institute of Structural Biology') to D. Willbold.},
      abstract     = {Viral protein U (VpU) of HIV-1 plays an important role in
                      downregulation of the main HIV-1 receptor CD4 from the
                      surface of infected cells. Physical binding of VpU to newly
                      synthesized CD4 in the endoplasmic reticulum is an early
                      step in a pathway leading to proteasomal degradation of CD4.
                      In this study, regions in the cytoplasmic domain of VpU
                      involved in CD4 binding were identified by NMR spectroscopy.
                      Amino acids in both helices found in the cytoplasmic region
                      of VpU in membrane-mimicking detergent micelles experience
                      chemical shift perturbations upon binding to CD4, whereas
                      amino acids between the two helices and at the C-terminus of
                      VpU show no or only small changes, respectively. The
                      topology of the complex was further studied with
                      paramagnetic relaxation enhancement. Paramagnetic spin
                      labels were attached at three sequence positions of a CD4
                      peptide comprising the transmembrane and cytosolic domains
                      of the receptor. VpU binds to a membrane-proximal region in
                      the cytoplasmic domain of CD4.},
      keywords     = {J (WoSType)},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22863293},
      UT           = {WOS:000308928900016},
      doi          = {10.1111/j.1742-4658.2012.08732.x},
      url          = {https://juser.fz-juelich.de/record/22825},
}