8 research outputs found

    Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails-4

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    <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>an value is denoted as a solid line and the mean value plus one standard deviation as a dash line. () A ribbon diagram view mapping the binding interface of H4-AcK12 peptide on Brd2 BD2. The residues, whose combined chemical shift changes were more than the mean value plus one standard deviation and above the mean value, are colored in blue and cyan respectively. The figure B was generated in PyMOL

    Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails-5

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    <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>the unacetylated peptide H4-U. Combined chemical shift perturbation was calculated using the equation, , and R = [peptide]/[bromodomain]

    Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails-7

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    <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> more significant perturbed residue G335 during titrations was followed

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

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    <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 (▼)

    Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails-0

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    <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>representation of the average, energy-minimized structure with the secondary structure elements highlighted. The helix nomenclature follows that of hsP/CAF bromodomain [9]. () Contact surface emphasized surface hydrophobic potential (left) and surface electrostatic potential (right) at the acetyl-lysine binding site. Yellow denotes hydrophobic potential; red negative potential; and blue positive potential. () A clear view of showing the conserved or type conserved side chains lined the hydrophobic cavity, and denoting the negative-charged collar formed by residues D330, D338, D341, D385 and D387. A, B, C and D were produced with MOLMOL or PyMOL

    Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails-2

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    <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>of Brd2 BD1 (pink) [PDB: ]. The figure was generated with MOLMOL

    Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails-8

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    <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>as a function of residue number of Brd2 BD2. Only those residues of which H-N cross-peaks are resolved enough to permit accurate measurements of their intensities are included

    Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails-1

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    <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>N5, 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 (▼)
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