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 high-tech, dedicated method is applied to construct targeted 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.
Several key aspects differentiate our library:
partner
Reaxense
upacc
Q9BYC5
UPID:
FUT8_HUMAN
Alternative names:
Fucosyltransferase 8; GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase; GDP-fucose--glycoprotein fucosyltransferase; Glycoprotein 6-alpha-L-fucosyltransferase
Alternative UPACC:
Q9BYC5; B4DFS7; G3V5N0; O00235; Q8IUA5; Q9BYC6; Q9P2U5; Q9P2U6
Background:
Alpha-(1,6)-fucosyltransferase, also known as Fucosyltransferase 8, plays a pivotal role in glycoprotein biosynthesis. It catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue on N-glycans. This enzymatic activity is crucial for the proper function and structural integrity of glycoproteins, which are involved in numerous cellular processes.
Therapeutic significance:
The enzyme's dysfunction is linked to Congenital disorder of glycosylation with defective fucosylation 1, characterized by developmental delays, skeletal anomalies, and immunodeficiency. Understanding the role of Alpha-(1,6)-fucosyltransferase could open doors to potential therapeutic strategies for this disorder and related glycosylation abnormalities.