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@ARTICLE{Haenel:55020,
      author       = {Haenel, K. and Stangler, T. and Stoldt, M. and Willbold,
                      D.},
      title        = {{S}olution structure of the {X}4 protein coded by the
                      {SARS} related coronavirus reveals an immunoglobulin like
                      fold and suggests a binding activity to integrin {I}
                      domains},
      journal      = {Journal of biomedical science},
      volume       = {13},
      issn         = {1021-7770},
      address      = {London},
      publisher    = {BioMed Central},
      reportid     = {PreJuSER-55020},
      pages        = {281 - 293},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The SARS related Coronavirus genome contains a variety of
                      novel accessory genes. One of these, called ORF7a or ORF8,
                      code for a protein, known as 7a, U122 or X4. We set out to
                      determine the three-dimensional structure of the soluble
                      ectodomain of this type-I transmembrane protein by nuclear
                      magnetic resonance spectroscopy. The fold of the protein is
                      the first member of a further variation of the
                      immunoglobulin like beta-sandwich fold. Because X4 does not
                      reveal significant sequence homologies to proteins in the
                      data bases, we carried out a structure based similarity
                      search for proteins with known function. High structural
                      similarity to Dl domains of ICAM-1 and ICAM-2, and common
                      features in amino acid sequence between X4 and ICAM-1,
                      suggest X4 to possess binding activity for the alpha(L)
                      integrin I domain of LFA-1. Further, based on this structure
                      based prediction, potential functions of X4 in virus
                      replication and pathogenesis are discussed.},
      keywords     = {Amino Acid Sequence / Antigens, CD: chemistry / Cell
                      Adhesion Molecules: chemistry / Cloning, Molecular / Humans
                      / Immunoglobulins: chemistry / Integrins: chemistry /
                      Intercellular Adhesion Molecule-1: chemistry /
                      Interleukin-1: chemistry / Lymphocyte Function-Associated
                      Antigen-1: chemistry / Models, Molecular / Molecular
                      Sequence Data / Open Reading Frames / Protein Structure,
                      Secondary / Protein Structure, Tertiary / SARS Virus:
                      chemistry / Viral Matrix Proteins: chemistry / Viral
                      Proteins: chemistry / Antigens, CD (NLM Chemicals) / Cell
                      Adhesion Molecules (NLM Chemicals) / Immunoglobulins (NLM
                      Chemicals) / Integrins (NLM Chemicals) / Interleukin-1 (NLM
                      Chemicals) / Lymphocyte Function-Associated Antigen-1 (NLM
                      Chemicals) / Viral Matrix Proteins (NLM Chemicals) / Viral
                      Proteins (NLM Chemicals) / sars7a protein, SARS virus (NLM
                      Chemicals) / Intercellular Adhesion Molecule-1 (NLM
                      Chemicals) / ICAM2 protein, human (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBI-2},
      ddc          = {610},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Medicine, Research $\&$ Experimental},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16328780},
      UT           = {WOS:000237502100001},
      doi          = {10.1007/s11373-005-9043-9},
      url          = {https://juser.fz-juelich.de/record/55020},
}