CREB Binding Protein (CREBBP) is a coactivator of transcription factor CREB that activates genes in cAMP transcriptional pathway. The coactivator binds to transcription factor activation domains positions histone acetyltransferases near specific nucleosomes in target gene promoter regions, recognizing the acetylated lysine residue.

Our Halogen-Enriched Fragment Library comprises 708 brominated fragments that can explore binding sites for favorable halogen bond interactions to identify unique binding modes that are complementary to those obtained from classical fragment-based screening.
 

Fragment-based lead design (FBLD) could be used to identify new metal-binding groups for metalloenzyme inhibitors. Several small-molecule chelators have been shown to effectively inhibit metalloproteins, therefore the design,

Enzymes involved in the epigenetic regulation of the genome represent promising starting points for therapeutic intervention by small molecules, and DNA methyltransferases (DNMT) are emerging targets for the development of a new class of cancer therapeutics.

Epigenetic regulators are new popular targets for cancer treatment. One of the promising epigenetic drug targets is Bromodomain-containing Protein 4 (BRD4) that binds to acetylated histone lysine residues and stimulates transcriptional elongation leading to expression of growth-promoting genes. 

UPDATED! The library has been just updated!
The central purpose of this specially designed Fragment Library is to provide