Explore the Potential with AI-Driven Innovation
The specialised, focused library is developed on demand with the most recent virtual screening and parameter assessment technology, guided by the Receptor.AI drug discovery platform. This approach exceeds the capabilities of traditional methods and offers compounds with higher 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 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
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.
Our library stands out due to several important features:
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.