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.
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.
The library includes a list of the most effective modulators, each annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Furthermore, each compound is shown with its optimal docking poses, affinity scores, and activity scores, offering a detailed summary.
Our top-notch dedicated system is used to design specialised libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology leverages molecular simulations to examine a vast array of proteins, capturing their dynamics in both isolated forms and in complexes with other proteins. Through ensemble virtual screening, we thoroughly account for the protein's conformational mobility, identifying critical binding sites within functional regions and distant allosteric locations. This detailed exploration ensures that we comprehensively assess every possible mechanism of action, with the objective of identifying novel therapeutic targets and lead compounds that span a wide spectrum of biological functions.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q15646
UPID:
OASL_HUMAN
Alternative names:
2'-5'-OAS-related protein; 59 kDa 2'-5'-oligoadenylate synthase-like protein; Thyroid receptor-interacting protein 14; p59 OASL
Alternative UPACC:
Q15646; B2RAZ2; I1YDD2; O75686; Q17R95; Q9Y6K6; Q9Y6K7
Background:
The 2'-5'-oligoadenylate synthase-like protein, known by alternative names such as 2'-5'-OAS-related protein and p59 OASL, plays a crucial role in the innate immune response. Despite lacking 2'-5'-OAS activity, it binds double-stranded RNA and exhibits antiviral activity against viruses like EMCV and HCV through an alternative pathway independent of RNase L.
Therapeutic significance:
Understanding the role of 2'-5'-oligoadenylate synthase-like protein could open doors to potential therapeutic strategies. Its unique mechanism of action in antiviral defense highlights its potential as a target for developing novel antiviral therapies.