Sandbox Reserved 896: Difference between revisions
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[[Image:BRD2BD1SurfaceView.png]] | [[Image:BRD2BD1SurfaceView.png]] | ||
Figure 1: Surface view of BD1 binding N-acetyl-lysine 12 of histone H4. The hypoacetylated side chain of lysine 8 that coordinates the dimer interface cannot be seen in this figure. Figure produced by PyMol (PDB ID: 2DVQ). | Figure 1: Surface view of BD1 binding N-acetyl-lysine 12 of histone H4. The hypoacetylated side chain of lysine 8 that coordinates the dimer interface cannot be seen in this figure. Figure produced by PyMol (PDB ID: 2DVQ) [17]. | ||
== Structure == | == Structure == | ||
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[[Image:BD1HomodimerTertiaryStructure.png]] | [[Image:BD1HomodimerTertiaryStructure.png]] | ||
Figure 2: Tertiary Structure of BRD2-BD1 in complex with N-acetyl-lysine 12 of histone H4. Figure produced by PyMol (PDB ID: 2DVQ) | Figure 2: Tertiary Structure of BRD2-BD1 in complex with N-acetyl-lysine 12 of histone H4. Figure produced by PyMol (PDB ID: 2DVQ) [17]. | ||
== Medical Relevance == | == Medical Relevance == | ||
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[[Image:BD1BD2Alignment.png]] | [[Image:BD1BD2Alignment.png]] | ||
Sequences derived from Uniprot. Figure produced by Clustal Omega | Sequences derived from Uniprot. Figure produced by Clustal Omega [18]. | ||
Key: P25440 (91-163) = BRD2-BD1; P25440 (364-463) = BRD2-BD2; * = identical residue; . = chemically similar residue; : = very chemically similar residue | Key: P25440 (91-163) = BRD2-BD1; P25440 (364-463) = BRD2-BD2; * = identical residue; . = chemically similar residue; : = very chemically similar residue | ||
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[[Image:BD1Alignment.png]] | [[Image:BD1Alignment.png]] | ||
Sequences derived from Uniprot. Figure produced by Clustal Omega. | Sequences derived from Uniprot. Figure produced by Clustal Omega [18]. | ||
Key: P25440 = BRD2; Q15059 = BRD3; O60885 = BRD4; Q58F21 = BRDT; * = identical residue; . = chemically similar residue; : = very chemically similar residue. | Key: P25440 = BRD2; Q15059 = BRD3; O60885 = BRD4; Q58F21 = BRDT; * = identical residue; . = chemically similar residue; : = very chemically similar residue. | ||
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[[Image:BD2Alignment.png]] | [[Image:BD2Alignment.png]] | ||
Sequences derived from Uniprot. Figure produced by Clustal Omega | Sequences derived from Uniprot. Figure produced by Clustal Omega [18]. | ||
Key: P25440 = BRD2; Q15059 = BRD3; O60885 = BRD4; Q58F21 = BRDT; * = identical residue; . = chemically similar residue; : = very chemically similar residue. | Key: P25440 = BRD2; Q15059 = BRD3; O60885 = BRD4; Q58F21 = BRDT; * = identical residue; . = chemically similar residue; : = very chemically similar residue. | ||
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[[Image:NETAlignment.png]] | [[Image:NETAlignment.png]] | ||
Sequences derived from Uniprot. Figure produced by Clustal Omega. | Sequences derived from Uniprot. Figure produced by Clustal Omega [18]. | ||
Key: P25440 = BRD2; Q15059 = BRD3; O60885 = BRD4; Q58F21 = BRDT; * = identical residue; . = chemically similar residue; : = very chemically similar residue. | Key: P25440 = BRD2; Q15059 = BRD3; O60885 = BRD4; Q58F21 = BRDT; * = identical residue; . = chemically similar residue; : = very chemically similar residue. | ||
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[16] Notredame C, Higgins DG, Heringa J. T-coffee: a novel method for fast and accurate multiple sequence alignment. Thornton J, editor. Journal of Molecular Biology. 2000;302(1):205–17. | [16] Notredame C, Higgins DG, Heringa J. T-coffee: a novel method for fast and accurate multiple sequence alignment. Thornton J, editor. Journal of Molecular Biology. 2000;302(1):205–17. | ||
[17] The PyMOL Molecular Graphics System, Version 1.2r3pre, Schrödinger, LLC. | |||
[18] 18. Sievers F, Higgins DG. Clustal Omega, Accurate Alignment of Very Large Numbers of Sequences. Methods in Molecular Biology Multiple Sequence Alignment Methods. 2013;:105–16. | |||
<references/> | <references/> | ||