Explore the Potential with AI-Driven Innovation
This comprehensive focused library is produced on demand with state-of-the-art virtual screening and parameter assessment technology driven by Receptor.AI drug discovery platform. This approach outperforms traditional methods and provides higher-quality compounds with superior 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 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
The method includes detailed molecular simulations of the catalytic and allosteric binding pockets, along with ensemble virtual screening that considers their conformational flexibility. In the design of modulators, structural changes induced by reaction intermediates are taken into account to enhance activity and selectivity.
Key features that set our library apart include:
partner
Reaxense
upacc
Q86XT4
UPID:
TRI50_HUMAN
Alternative names:
RING-type E3 ubiquitin transferase TRIM50; Tripartite motif-containing protein 50
Alternative UPACC:
Q86XT4; Q2M204; Q86XT3
Background:
E3 ubiquitin-protein ligase TRIM50, also known as RING-type E3 ubiquitin transferase TRIM50 and Tripartite motif-containing protein 50, plays a pivotal role in cellular processes. It ubiquitinates Beclin-1/BECN1, enhancing its binding to ULK1 and promoting starvation-induced autophagy activation. Additionally, it interacts with p62/SQSTM1, facilitating the autophagy clearance of aggresome-associated polyubiquitinated proteins through HDAC6 interaction. TRIM50 also activates the NLRP3 inflammasome by inducing NLRP3 oligomerization, independent of its E3 ligase function.
Therapeutic significance:
Understanding the role of E3 ubiquitin-protein ligase TRIM50 could open doors to potential therapeutic strategies.