Explore the Potential with AI-Driven Innovation
This extensive focused library is tailor-made using the latest virtual screening and parameter assessment technology, operated by the Receptor.AI drug discovery platform. This technique is more effective than traditional methods, offering compounds with improved activity, selectivity, and safety.
Our selection of compounds is from a large virtual library of over 60 billion molecules. The production and distribution of these compounds are managed by our partner Reaxense.
Contained in the library are leading modulators, each labelled with 38 ADME-Tox and 32 physicochemical and drug-likeness qualities. In addition, each compound is illustrated with its optimal docking poses, affinity scores, and activity scores, giving a complete picture.
We utilise our cutting-edge, exclusive workflow to develop focused libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The procedure entails thorough molecular simulations of the catalytic and allosteric binding pockets, accompanied by ensemble virtual screening that factors in their conformational flexibility. When developing modulators, the structural modifications brought about by reaction intermediates are factored in to optimize activity and selectivity.
Several key aspects differentiate our library:
partner
Reaxense
upacc
P17655
UPID:
CAN2_HUMAN
Alternative names:
Calcium-activated neutral proteinase 2; Calpain M-type; Calpain large polypeptide L2; Calpain-2 large subunit; Millimolar-calpain
Alternative UPACC:
P17655; A6NDG7; B7ZA96; E7ES58; Q16738; Q6PJT3; Q8WU26; Q9HBB1
Background:
Calpain-2 catalytic subunit, also known as Calcium-activated neutral proteinase 2, plays a crucial role in calcium-regulated non-lysosomal thiol-protease activities. It is instrumental in cytoskeletal remodeling and signal transduction, cleaving substrates like MYOC and CPEB3 to modulate their functions.
Therapeutic significance:
Understanding the role of Calpain-2 catalytic subunit could open doors to potential therapeutic strategies.