Explore the Potential with AI-Driven Innovation
The focused library is created on demand with the latest virtual screening and parameter assessment technology, supported by the Receptor.AI drug discovery platform. This method is more effective than traditional methods and results in higher-quality compounds with better activity, selectivity, and safety.
We pick out particular compounds from an extensive virtual database of more than 60 billion molecules. The preparation and shipment of these compounds are facilitated by our associate Reaxense.
The library includes a list of the most promising modulators annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Also, each compound is presented with its optimal docking poses, affinity scores, and activity scores, providing a comprehensive overview.
We employ our advanced, specialised process to create targeted 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.
Our library stands out due to several important features:
partner
Reaxense
upacc
P20718
UPID:
GRAH_HUMAN
Alternative names:
CCP-X; Cathepsin G-like 2; Cytotoxic T-lymphocyte proteinase; Cytotoxic serine protease C
Alternative UPACC:
P20718; G3V2C5; Q6XGZ0; Q6XGZ1
Background:
Granzyme H, also known as CCP-X, Cathepsin G-like 2, Cytotoxic T-lymphocyte proteinase, and Cytotoxic serine protease C, is a chymotrypsin-like serine protease. It exhibits a preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites, playing a crucial role in target cell lysis during cell-mediated immune responses. Additionally, it is involved in the antiviral response by directly cleaving several proteins essential for viral replication.
Therapeutic significance:
Understanding the role of Granzyme H could open doors to potential therapeutic strategies.