Human Kinases Annotated Library

Kinases mediate the transfer of a phosphate moiety from a high energy molecule (such as ATP) to their substrate molecule. Kinases are needed to stabilize this reaction because the phosphoanhydride bond contains a high level of energy. Kinases properly orient their substrate and the phosphoryl group within their active sites, which increases the rate of the reaction. Additionally, they commonly use positively charged amino acid residues, which electrostatically stabilize the transition state by interacting with the negatively charged phosphate groups. Alternatively, some kinases utilize bound metal cofactors in their active sites to coordinate the phosphate groups. Protein kinases can be classed as catalytically active (canonical) or as pseudokinases, reflecting the evolutionary loss of one or more of the catalytic amino acids that position or hydrolyse ATP.

Human Kinases Annotated Library

2,500 Compounds

• Kinases are enzymatic proteins that phosphorylate other functional proteins
• Physiologically the kinase enzymatic activity can be modulated by
– Catalytic ATP site binders
– Allosteric binders that cause conformational changes within the catalytic ATP site
• Kinases are well recognized as important therapeutic targets for
– Oncology, e.g. cancer immunotherapy
– Inflammatory diseases, e.g. fibrosis, rheumatoid arthritis
– Cardiovascular system, e.g. cerebral vasospasm, pulmonary arterial hypertension
A unique collection of small molecule compounds with annotated activities for Kinases protein targets
❑ Annotated activities : 236 kinase targets
❑ Express Delivery : 640 compounds
❑ Complete Version : 2585 compounds

Medicinal and Computational Chemistry Dept., ChemDiv, Inc.
12760 High Bluff Dr, San Diego, CA, 92130
Phone: + 1 916 234 0888
Fax: +1 858 794 4931
Email: ChemDiv@chemdiv.com

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