Publication: Structured water molecules in the binding site of bromodomains can be displaced by cosolvent
Structured water molecules in the binding site of bromodomains can be displaced by cosolvent
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Huang, D., Rossini, E., Steiner, S., & Caflisch, A. (2013). Structured water molecules in the binding site of bromodomains can be displaced by cosolvent. ChemMedChem, 9(3), 573–579. https://doi.org/10.1002/cmdc.201300156
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Bromodomains are α-helical bundles of approximately 110 residues that recognize acetylated lysine side chains mainly on histone tails. Bromodomains are known to play an important role in cancer and inflammation, and as such, significant efforts are being made to identify small-molecule inhibitors of these epigenetic reader proteins. Here, explicit solvent molecular dynamics (MD) simulations of two bromodomains (BAZ2B and CREBBP) are used to analyze the water molecules that seem to be conserved at the bottom of the acetyl-lysine bindin
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- Huang, Danzhi
- Rossini, Emanuele
- Steiner, Sandra
- Caflisch, Amedeo
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Huang, D., Rossini, E., Steiner, S., & Caflisch, A. (2013). Structured water molecules in the binding site of bromodomains can be displaced by cosolvent. ChemMedChem, 9(3), 573–579. https://doi.org/10.1002/cmdc.201300156
