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@ARTICLE{Wittlich:7147,
      author       = {Wittlich, M. and Thiagarajan, P. and Koenig, B. W. and
                      Hartmann, R. and Willbold, D.},
      title        = {{NMR} structure of the transmembrane and cytoplasmic
                      domains of human {CD}4 in micelles},
      journal      = {Biochimica et biophysica acta},
      volume       = {1798},
      issn         = {0006-3002},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-7147},
      pages        = {122 - 127},
      year         = {2010},
      note         = {This work has been supported by a grant from the
                      "Prasidentenfond der Helmholtzgemeinschaft" (HGF, "Virtual
                      Institute of Structural Biology") to D.W.},
      abstract     = {The human cluster determinant 4 (CD4) is a type I
                      transmembrane glycoprotein involved in T-cell signalling. It
                      is expressed primarily on the surface of T helper cells but
                      also on subsets of memory and regulatory T lymphocytes
                      (CD4(+) cells). It serves as a coreceptor in T-cell receptor
                      recognition of MHC II antigen complexes. Besides its
                      cellular functions, CD4 serves as the main receptor for
                      human immunodeficiency virus type I (HIV-1). During T-cell
                      infection, the CD4 extracellular domain is bound by HIV-1
                      gp120, the viral surface glycoprotein, which triggers a
                      number of conformational changes ultimately resulting in
                      virion entry of the cell. Subsequently, CD4 is downregulated
                      in infected cells by multiple strategies that involve direct
                      interactions of the HIV-1 proteins VpU and Nef with the
                      cytoplasmic part of CD4. In the present work, we describe
                      the NOE-based solution structure of the transmembrane and
                      cytoplasmic domains of the cystein-free variant of CD4
                      (CD4mut) in dodecylphosphocholine (DPC) micelles.
                      Furthermore, we have characterized micelle-inserted CD4mut
                      by paramagentic relaxation enhancement (PRE) agents and
                      (1)H-(15)N heteronuclear NOE data. CD4mut features a stable
                      and well-defined transmembrane helix from M372 to V395
                      buried in the micellar core and a cytoplasmic helix ranging
                      from A404 to L413. Experimental data suggest the amphipathic
                      cytoplasmic helix to be in close contact with the micellar
                      surface. The role of the amphipathic helix and its
                      interaction with the micellar surface is discussed with
                      respect to the biological function of the full-length CD4
                      protein.},
      keywords     = {Antigens, CD4: chemistry / Antigens, CD4: immunology /
                      Antigens, CD4: metabolism / Humans / Micelles / Nuclear
                      Magnetic Resonance, Biomolecular: methods /
                      Phosphorylcholine: analogs $\&$ derivatives /
                      Phosphorylcholine: chemistry / Phosphorylcholine: metabolism
                      / Protein Structure, Secondary: physiology / Protein
                      Structure, Tertiary: physiology / Antigens, CD4 (NLM
                      Chemicals) / Micelles (NLM Chemicals) / Phosphorylcholine
                      (NLM Chemicals) / dodecylphosphocholine (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      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 / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19781520},
      UT           = {WOS:000274859300009},
      doi          = {10.1016/j.bbamem.2009.09.010},
      url          = {https://juser.fz-juelich.de/record/7147},
}