Explore the Potential with AI-Driven Innovation
This extensive focused library is tailor-made using the latest virtual screening and parameter assessment technology, operated by the Receptor.AI drug discovery platform. This technique is more effective than traditional methods, offering compounds with improved 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.
Contained in the library are leading modulators, each labelled with 38 ADME-Tox and 32 physicochemical and drug-likeness qualities. In addition, each compound is illustrated with its optimal docking poses, affinity scores, and activity scores, giving a complete picture.
Our top-notch dedicated system is used to design specialised 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 is unique due to several crucial aspects:
partner
Reaxense
upacc
O96028
UPID:
NSD2_HUMAN
Alternative names:
Multiple myeloma SET domain-containing protein; Nuclear SET domain-containing protein 2; Protein trithorax-5; Wolf-Hirschhorn syndrome candidate 1 protein
Alternative UPACC:
O96028; A2A2T2; A2A2T3; A2A2T4; A7MCZ1; D3DVQ2; O96031; Q4VBY8; Q672J1; Q6IS00; Q86V01; Q9BZB4; Q9UI92; Q9UPR2
Background:
Histone-lysine N-methyltransferase NSD2, also known as Multiple myeloma SET domain-containing protein, plays a pivotal role in chromatin remodeling and gene expression regulation. It specifically dimethylates histone H3 at 'Lys-36', influencing various biological processes including adipogenesis, T-cell activation, and B-cell development.
Therapeutic significance:
Mutations in NSD2 are linked to Rauch-Steindl syndrome, characterized by growth retardation and developmental delays. Understanding the role of NSD2 could open doors to potential therapeutic strategies for this disorder.