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.


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