Image:Screen shot 2013-05-07 at 2.01.54 PM.png
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Cartoon showing the solution structure of the bromodomain of human BRPF1 in complex with histone H4K5ac peptide (PDB2RS9). Like all known bromodomains, the BRPF1 bromodamain adopts a conserved structural fold of a left-handed bundle of four helices (αZ, αA, αB, and αC ) with the inter-helical ZA and BC loops having variable length and sequence. This variable regions make a hydrophobic pocket constituting the binding site.
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| Date/Time | User | Dimensions | File size | Comment | |
|---|---|---|---|---|---|
| (current) | 19:40, 7 May 2013 | Mulu Lubula (Talk | contribs) | 494×396 | 41 KB | Cartoon showing the solution structure of the bromodomain of human BRPF1 in complex with histone H4K5ac peptide (PDB:2RS9).Like all known bromodomains, the BRPF1 bromodamain adopts a conserved structural fold of a left-handed bundle of four helices (αZ, |
| 19:30, 7 May 2013 | Mulu Lubula (Talk | contribs) | 494×396 | 41 KB | Cartoon showing the solution structure of the bromodomain of human BRPF1 in complex with histone H4K5ac peptide (PDB2RS9). Like all known bromodomains, the BRPF1 bromodamain adopts a conserved structural fold of a left-handed bundle of four helices (αZ, |
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