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000128162 0247_ $$2doi$$a10.3390/biology1020277
000128162 0247_ $$2Handle$$a2128/8842
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000128162 037__ $$aFZJ-2012-01057
000128162 041__ $$aEnglish
000128162 082__ $$a570
000128162 1001_ $$0P:(DE-HGF)0$$aQuy, Vo Cam$$b0$$eCorresponding author
000128162 245__ $$aHIV-1 Tat Binding to PCAF Bromodomain: Structural Determinants from Computational Methods
000128162 260__ $$aBasel$$bMDPI$$c2012
000128162 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s128162
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000128162 520__ $$aThe 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.
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000128162 588__ $$aDataset connected to CrossRef, juser.fz-juelich.de
000128162 7001_ $$0P:(DE-HGF)0$$aPantano, Sergio$$b1
000128162 7001_ $$0P:(DE-HGF)0$$aGiacca, Mauro$$b3
000128162 7001_ $$0P:(DE-Juel1)145921$$aRossetti, Giulia$$b2$$ufzj
000128162 7001_ $$0P:(DE-Juel1)145614$$aCarloni, Paolo$$b4$$eCorresponding Author$$ufzj
000128162 770__ $$aStructural and Molecular Biology of HIV
000128162 773__ $$0PERI:(DE-600)2661517-4$$a10.3390/biology1020277$$gVol. 1, no. 3, p. 277 - 296$$n2$$p277 - 296$$tBiology$$v1$$x2079-7737$$y2012
000128162 8564_ $$yPublished under CreativeCommons License$$zPublished final document.
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000128162 9141_ $$y2012
000128162 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)145921$$aForschungszentrum Jülich GmbH$$b2$$kFZJ
000128162 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)145614$$aForschungszentrum Jülich GmbH$$b4$$kFZJ
000128162 9101_ $$0I:(DE-588b)1026307295$$6P:(DE-HGF)0$$aGerman Research School for Simulation Sciences$$b0$$kGRS
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