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@ARTICLE{Briese:49422,
      author       = {Briese, L. and Preusser-Kunze, A. and Willbold, D.},
      title        = {{M}apping the binding site of full length {HIV}-1 {N}ef on
                      human {L}ck {SH}3 by {NMR} spectroscopy},
      journal      = {Journal of biomedical science},
      volume       = {12},
      issn         = {1021-7770},
      address      = {London},
      publisher    = {BioMed Central},
      reportid     = {PreJuSER-49422},
      pages        = {451 - 456},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The Nef protein of human immunodeficiency virus type 1
                      (HIV-1) is known to directly bind to the SH3 domain of human
                      lymphocyte specific kinase (Lck) via a proline-rich region
                      located in the amino terminal part of Nef. To address the
                      question whether Nef binding to Lck SH3 involves residues
                      outside the typical poly-proline peptide binding site and
                      whether the Lck unique domain is involved in Nef-Lck
                      interaction, we studied the direct interaction between both
                      molecules using recombinant full-length HIV-1 Nef protein on
                      one side and recombinantly expressed and uniformly
                      15N-isotope labeled Lck protein comprising unique and SH3
                      domains on the other side. Applying nuclear magnetic
                      resonance spectroscopy we could show that only residues of
                      Lck SH3, that are typically involved in binding poly-proline
                      peptides, are affected by Nef binding. Further, for the
                      first time we could rule out that residues of Lck unique
                      domain are involved in binding to full length Nef protein.
                      Thus, interactions of Lck unique domain to cellular partners
                      e.g. CD4 or CD8, are not necessarily competitive with Lck
                      binding to HIV-1 Nef.},
      keywords     = {Amino Acid Sequence / Binding Sites / Gene Products, nef:
                      chemistry / HIV-1: chemistry / HIV-1: metabolism / Humans /
                      Lymphocyte Specific Protein Tyrosine Kinase p56(lck):
                      chemistry / Magnetic Resonance Spectroscopy / Models,
                      Molecular / Molecular Sequence Data / Protein Interaction
                      Mapping / Protein Structure, Tertiary / Receptors, Virus:
                      metabolism / Recombinant Proteins / nef Gene Products, Human
                      Immunodeficiency Virus / src Homology Domains / Gene
                      Products, nef (NLM Chemicals) / Receptors, Virus (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals) / nef Gene
                      Products, Human Immunodeficiency Virus (NLM Chemicals) /
                      Lymphocyte Specific Protein Tyrosine Kinase p56(lck) (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {610},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Medicine, Research $\&$ Experimental},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15976924},
      UT           = {WOS:000230695300002},
      doi          = {10.1007/s11373-005-6797-z},
      url          = {https://juser.fz-juelich.de/record/49422},
}