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@ARTICLE{Wittlich:60128,
      author       = {Wittlich, M. and Koenig, B. W. and Hoffmann, S. and
                      Willbold, D.},
      title        = {{S}tructural characterisation of the transmembrane and
                      cytoplasmic domains of human {CD}4},
      journal      = {Biochimica et biophysica acta / Biomembranes},
      volume       = {1768},
      issn         = {0005-2736},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-60128},
      pages        = {2949 - 2960},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Cluster determinant 4 (CD4) is a type I transmembrane
                      glycoprotein of 58 kDa. It consists of an extracellular
                      domain of 370 amino acids, a short transmembrane region, and
                      a cytoplasmic domain of 40 amino acids at the C-terminal
                      end. We investigated the structure of the 62 C-terminal
                      residues of CD4, comprising its transmembrane and
                      cytoplasmic domains. The five cysteine residues of this
                      region have been replaced with serine and histidine residues
                      in the polypeptide CD4mut. Uniformly 15N and 13C labeled
                      protein was recombinantly expressed in E. coli and purified.
                      Functional binding activity of CD4mut to protein VpU of the
                      human immunodeficiency virus type 1 (HIV-1) was verified.
                      Close to complete NMR resonance assignment of the 1H, 13C,
                      and 15N spins of CD4mut was accomplished. The secondary
                      structure of CD4mut in membrane simulating
                      dodecylphosphocholine (DPC) micelles was characterized based
                      on secondary chemical shift analysis, NOE-based
                      proton-proton distances, and circular dichroism
                      spectroscopy. A stable transmembrane helix and a short
                      amphipathic helix in the cytoplasmic region were identified.
                      The fractional helicity of the cytoplasmic helix appears to
                      be stabilized in the presence of DPC micelles, although the
                      extension of this helix is reduced in comparison to previous
                      studies on synthetic peptides in aqueous solution. The role
                      of the amphipathic helix and its potentially variable length
                      is discussed with respect to the biological functions of
                      CD4.},
      keywords     = {Amino Acid Sequence / Antigens, CD4: chemistry / Antigens,
                      CD4: genetics / Antigens, CD4: metabolism / Carbon Isotopes
                      / Circular Dichroism / Human Immunodeficiency Virus
                      Proteins: metabolism / Humans / Magnetic Resonance
                      Spectroscopy: methods / Models, Molecular / Molecular
                      Sequence Data / Mutation / Nitrogen Isotopes / Protein
                      Binding / Protein Structure, Secondary / Protein Structure,
                      Tertiary / Viral Regulatory and Accessory Proteins:
                      metabolism / Antigens, CD4 (NLM Chemicals) / Carbon Isotopes
                      (NLM Chemicals) / Human Immunodeficiency Virus Proteins (NLM
                      Chemicals) / Nitrogen Isotopes (NLM Chemicals) / Viral
                      Regulatory and Accessory Proteins (NLM Chemicals) / J
                      (WoSType)},
      cin          = {INB-2 / JARA-SIM},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805 / I:(DE-Juel1)VDB1045},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18035040},
      UT           = {WOS:000252488900002},
      doi          = {10.1016/j.bbamem.2007.10.023},
      url          = {https://juser.fz-juelich.de/record/60128},
}