Publication: Binding Mode of Acetylated Histones to Bromodomains: Variations on a Common Motif
Binding Mode of Acetylated Histones to Bromodomains: Variations on a Common Motif
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Marchand, J.-R., & Caflisch, A. (2015). Binding Mode of Acetylated Histones to Bromodomains: Variations on a Common Motif. ChemMedChem, 10(8), 1327–1333. https://doi.org/10.1002/cmdc.201500141
Abstract
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Bromodomains, epigenetic readers that recognize acetylated lysine residues in histone tails, are potential drug targets in cancer and inflammation. Herein we review the crystal structures of human bromodomains in complex with histone tails and analyze the main interaction motifs. The histone backbone is extended and occupies, in one of the two possible orientations, the bromodomain surface groove lined by the ZA and BC loops. The acetyl-lysine side chain is buried in the cavity between the four helices of the bromodomain, and its oxyg
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- Marchand, Jean-Rémy
- Caflisch, Amedeo
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Marchand, J.-R., & Caflisch, A. (2015). Binding Mode of Acetylated Histones to Bromodomains: Variations on a Common Motif. ChemMedChem, 10(8), 1327–1333. https://doi.org/10.1002/cmdc.201500141
