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@ARTICLE{Sgobba:202096,
      author       = {Sgobba, Miriam and Olubiyi, Olujide and Ke, Song and
                      Haider, Shozeb},
      title        = {{M}olecular dynamics of {HIV}1-integrase in complex with
                      93del - a structural perspective on the mechanism of
                      inhibition.},
      journal      = {Caryologia},
      volume       = {29},
      number       = {5},
      issn         = {1538-0254},
      address      = {Abingdon, Oxon},
      publisher    = {Taylor $\&$ Francis63883},
      reportid     = {FZJ-2015-04385},
      pages        = {863 - 877},
      year         = {2012},
      abstract     = {HIV1 integrase is an important target for the antiviral
                      therapy. Guanine-rich quadruplex, such as 93del, have been
                      shown to be potent inhibitors of this enzyme and thus
                      representing a new class of antiviral agents. Although X-ray
                      and NMR structures of HIV1 integrase and 93del have been
                      reported, there is no structural information of the complex
                      and the mechanism of inhibition still remains unexplored. A
                      number of computational methods including automated
                      protein-DNA docking and molecular dynamics simulation in
                      explicit solvent were used to model the binding of 93del to
                      HIV1 integrase. Analysis of the dynamic behaviour of the
                      complex using principal components analysis and elastic
                      network modelling techniques allow us to understand how the
                      binding of 93del aptamer and its interactions with key
                      residues affect the intrinsic motions of the catalytic loops
                      by stabilising them in catalytically inactive conformations.
                      Such insights into the structural mechanism of inhibition
                      can aid in improving the design of anti-HIV aptamers.},
      keywords     = {Aptamers, Nucleotide (NLM Chemicals) / HIV Integrase
                      Inhibitors (NLM Chemicals) / p31 integrase protein, Human
                      immunodeficiency virus 1 (NLM Chemicals) / HIV Integrase
                      (NLM Chemicals)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22292948},
      UT           = {WOS:000300074600002},
      doi          = {10.1080/07391102.2012.10507418},
      url          = {https://juser.fz-juelich.de/record/202096},
}