Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails-10

Abstract

<p><b>Copyright information:</b></p><p>Taken from "Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails"</p><p>http://www.biomedcentral.com/1472-6807/7/57</p><p>BMC Structural Biology 2007;7():57-57.</p><p>Published online 12 Sep 2007</p><p>PMCID:PMC2065866.</p><p></p>5, hsCBP, hsP/CAF, hsBRG1 and the two components from TAF250. The sequences were aligned based on the experimentally determined three-dimensional structures of these bromodomains, highlighted in green. The secondary structure of Brd2 BD2 is indicated above the alignment. Residues identical in all sequences are shown in red and residues conserved are coloured in blue and residues corresponding to Z sheet (hsBRG1) and helix D are represented in yellow. The two amino acids insertion is indicated by triangle symbols (▼)