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@ARTICLE{Quy:128162,
      author       = {Quy, Vo Cam and Pantano, Sergio and Rossetti, Giulia and
                      Giacca, Mauro and Carloni, Paolo},
      title        = {{HIV}-1 {T}at {B}inding to {PCAF} {B}romodomain:
                      {S}tructural {D}eterminants from {C}omputational {M}ethods},
      journal      = {Biology},
      volume       = {1},
      number       = {2},
      issn         = {2079-7737},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2012-01057},
      pages        = {277 - 296},
      year         = {2012},
      abstract     = {The binding between the HIV-1 trans-activator of
                      transcription (Tat) and p300/(CREB-binding
                      protein)-associated factor (PCAF) bromodomain is a crucial
                      step in the HIV-1 life cycle. However, the structure of the
                      full length acetylated Tat bound to PCAF has not been yet
                      determined experimentally. Acetylation of Tat residues can
                      play a critical role in enhancing HIV-1 transcriptional
                      activation. Here, we have combined a fully flexible
                      protein-protein docking approach with molecular dynamics
                      simulations to predict the structural determinants of the
                      complex for the common HIV-1BRU variant. This model
                      reproduces all the crucial contacts between the Tat peptide
                      46SYGR(AcK)KRRQRC56 and the PCAF bromodomain previously
                      reported by NMR spectroscopy. Additionally, inclusion of the
                      entire Tat protein results in additional contact points at
                      the protein-protein interface. The model is consistent with
                      the available experimental data reported and adds novel
                      information to our previous structural predictions of the
                      PCAF bromodomain in complex with the rare HIVZ2 variant,
                      which was obtained with a less accurate computational
                      method. This improved characterization of Tat.PCAF
                      bromodomain binding may help in defining the structural
                      determinants of other protein interactions involving lysine
                      acetylation.},
      cin          = {JSC / GRS / IAS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)GRS-20100316 /
                      I:(DE-Juel1)IAS-5-20120330},
      pnm          = {411 - Computational Science and Mathematical Methods
                      (POF2-411)},
      pid          = {G:(DE-HGF)POF2-411},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24832227},
      doi          = {10.3390/biology1020277},
      url          = {https://juser.fz-juelich.de/record/128162},
}