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 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.
In the library, a selection of top modulators is provided, each marked with 38 ADME-Tox and 32 parameters related to physicochemical properties and drug-likeness. Also, every compound comes with its best docking poses, affinity scores, and activity scores, providing a comprehensive overview.
Our high-tech, dedicated method is applied to construct targeted 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.
Several key aspects differentiate our library:
partner
Reaxense
upacc
P26572
UPID:
MGAT1_HUMAN
Alternative names:
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
Alternative UPACC:
P26572; A8K404; B3KRU8; D3DWR1; Q6IBE3
Background:
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, also known as N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I, plays a pivotal role in the biosynthesis of complex N-linked carbohydrates. It is essential for the conversion of high-mannose to hybrid and complex N-glycans, a critical process in cellular functions and signaling.
Therapeutic significance:
Understanding the role of Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase could open doors to potential therapeutic strategies. Its involvement in the intricate process of glycan formation suggests its potential as a target in diseases where glycosylation patterns are disrupted.