Explore the Potential with AI-Driven Innovation
Our detailed focused library is generated on demand with advanced virtual screening and parameter assessment technology powered by the Receptor.AI drug discovery platform. This method surpasses traditional approaches, delivering compounds of better quality with enhanced activity, selectivity, and safety.
From a virtual chemical space containing more than 60 billion molecules, we precisely choose certain compounds. Our collaborator, Reaxense, aids in their synthesis and provision.
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.
We use our state-of-the-art dedicated workflow for designing focused libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The procedure entails thorough molecular simulations of the catalytic and allosteric binding pockets, accompanied by ensemble virtual screening that factors in their conformational flexibility. When developing modulators, the structural modifications brought about by reaction intermediates are factored in to optimize activity and selectivity.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q8IWV7
UPID:
UBR1_HUMAN
Alternative names:
N-recognin-1; RING-type E3 ubiquitin transferase UBR1; Ubiquitin-protein ligase E3-alpha-1; Ubiquitin-protein ligase E3-alpha-I
Alternative UPACC:
Q8IWV7; O60708; O75492; Q14D45; Q68DN9; Q8IWY6; Q96JY4
Background:
E3 ubiquitin-protein ligase UBR1, also known as N-recognin-1, plays a pivotal role in the N-end rule pathway of protein degradation. It specifically recognizes proteins with destabilizing N-terminal residues, marking them for ubiquitination and subsequent degradation. This process is crucial for maintaining cellular homeostasis and regulating protein levels.
Therapeutic significance:
UBR1's dysfunction is directly linked to Johanson-Blizzard syndrome, characterized by pancreatic insufficiency and developmental anomalies. Understanding UBR1's mechanisms offers a pathway to novel treatments for this syndrome and insights into pancreatic health.