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 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.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q96T88
UPID:
UHRF1_HUMAN
Alternative names:
Inverted CCAAT box-binding protein of 90 kDa; Nuclear protein 95; Nuclear zinc finger protein Np95; RING finger protein 106; RING-type E3 ubiquitin transferase UHRF1; Transcription factor ICBP90; Ubiquitin-like PHD and RING finger domain-containing protein 1; Ubiquitin-like-containing PHD and RING finger domains protein 1
Alternative UPACC:
Q96T88; A0JBR2; A8K024; B2RBA9; Q2HIX7; Q8J022; Q9H6S6; Q9P115; Q9P1U7
Background:
E3 ubiquitin-protein ligase UHRF1, also known as Nuclear protein 95 and Transcription factor ICBP90, is a pivotal epigenetic regulator. It bridges DNA methylation and chromatin modification, recognizing hemimethylated DNA and recruiting DNMT1 to ensure DNA methylation patterns are faithfully propagated. UHRF1's ability to bind histone H3 trimethylated at 'Lys-9' and unmethylated at 'Arg-2' facilitates chromatin protein recruitment, playing a crucial role in chromatin modification and transcription regulation.
Therapeutic significance:
Understanding the role of E3 ubiquitin-protein ligase UHRF1 could open doors to potential therapeutic strategies.