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 carefully select specific compounds from a vast collection of over 60 billion molecules in virtual chemical space. Our partner Reaxense helps in synthesizing and delivering these compounds.
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 high-tech, dedicated method is applied to construct targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
It includes comprehensive molecular simulations of the catalytic and allosteric binding pockets and the ensemble virtual screening accounting for their conformational mobility. In the case of designing modulators, the structural changes induced by reaction intermediates are taken into account to leverage activity and selectivity.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q7Z419
UPID:
R144B_HUMAN
Alternative names:
IBR domain-containing protein 2; RING finger protein 144B; p53-inducible RING finger protein
Alternative UPACC:
Q7Z419; B3KUA8; B4DZI2; Q5TB85; Q6P4Q0; Q8N3R7; Q9BX38
Background:
E3 ubiquitin-protein ligase RNF144B, also known as IBR domain-containing protein 2, RING finger protein 144B, and p53-inducible RING finger protein, plays a pivotal role in protein degradation. It functions by accepting ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 and transferring it to substrates like LCMT2 for degradation. This process is crucial for regulating apoptosis through a p53/TP53-dependent mechanism, albeit in a caspase-independent manner. Interestingly, RNF144B's overexpression can decrease the stability of BAX, a pro-apoptotic protein, thus protecting against cell death.
Therapeutic significance:
Understanding the role of E3 ubiquitin-protein ligase RNF144B could open doors to potential therapeutic strategies.