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 utilise our cutting-edge, exclusive workflow to develop focused 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.
Key features that set our library apart include:
partner
Reaxense
upacc
Q8NB78
UPID:
KDM1B_HUMAN
Alternative names:
Flavin-containing amine oxidase domain-containing protein 1; Lysine-specific histone demethylase 1B
Alternative UPACC:
Q8NB78; A2A2C5; A2A2C6; Q5TGV3; Q6AI15; Q6ZUU4; Q8N258; Q96EL7
Background:
Lysine-specific histone demethylase 2, also known as Flavin-containing amine oxidase domain-containing protein 1, plays a pivotal role in epigenetic transcriptional regulation by demethylating 'Lys-4' of histone H3. This action represses gene expression by removing a specific tag for transcriptional activation. It is essential for the methylation of certain imprinted genes during oogenesis, utilizing FAD to oxidize substrates for demethylation. Despite its specificity for mono- and di-methylated 'Lys-4', it does not affect tri-methylated 'Lys-4' or other methylated lysine residues on histones H3 and H4 without the aid of GLYR1.
Therapeutic significance:
Understanding the role of Lysine-specific histone demethylase 2 could open doors to potential therapeutic strategies.