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 features a range of promising modulators, each detailed with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Plus, each compound is presented with its ideal docking poses, affinity scores, and activity scores, ensuring a thorough insight.
We use our state-of-the-art dedicated workflow for designing focused libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
This approach involves comprehensive molecular simulations of the catalytic and allosteric binding pockets and ensemble virtual screening that accounts for their conformational flexibility. In the case of designing modulators, the structural adjustments caused by reaction intermediates are considered to improve activity and selectivity.
Key features that set our library apart include:
partner
Reaxense
upacc
Q96FW1
UPID:
OTUB1_HUMAN
Alternative names:
Deubiquitinating enzyme OTUB1; OTU domain-containing ubiquitin aldehyde-binding protein 1; Otubain-1; Ubiquitin-specific-processing protease OTUB1
Alternative UPACC:
Q96FW1; Q32Q78; Q96II3; Q9NXQ4; Q9P0B8
Background:
Ubiquitin thioesterase OTUB1, also known as Otubain-1, plays a crucial role in protein turnover by specifically removing 'Lys-48'-linked conjugated ubiquitin, thus preventing protein degradation. It regulates T-cell anergy through interaction with RNF128/GRAIL, influencing CD4 T-cell responsiveness. OTUB1 exhibits isoform-specific effects on RNF128, affecting T-cell anergy differently. Additionally, it deubiquitinates estrogen receptor alpha and mediates DNA repair regulation by inhibiting RNF168, thereby controlling the accumulation of 'Lys-63'-linked histone marks at DNA damage sites.
Therapeutic significance:
Understanding the role of Ubiquitin thioesterase OTUB1 could open doors to potential therapeutic strategies.