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 includes a list of the most promising modulators annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Also, each compound is presented with its optimal docking poses, affinity scores, and activity scores, providing a comprehensive overview.
We employ our advanced, specialised process to create targeted 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 distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q32P28
UPID:
P3H1_HUMAN
Alternative names:
Growth suppressor 1; Leucine- and proline-enriched proteoglycan 1
Alternative UPACC:
Q32P28; Q7KZR4; Q96BR8; Q96SK8; Q96SL5; Q96SN3; Q9H6K3; Q9HC86; Q9HC87
Background:
Prolyl 3-hydroxylase 1, also known as Growth suppressor 1 and Leucine- and proline-enriched proteoglycan 1, plays a pivotal role in collagen biosynthesis. It catalyzes the post-translational formation of 3-hydroxyproline in collagens, particularly types IV and V, which are essential for the structural integrity and function of connective tissues. This enzyme is also associated with the basement membrane and may influence cell secretory pathways and fibroblast growth suppression.
Therapeutic significance:
Prolyl 3-hydroxylase 1 is directly implicated in Osteogenesis imperfecta 8, a disorder characterized by bone fragility and susceptibility to fractures. The disease is linked to mutations affecting this enzyme, leading to severe collagen hydroxylation defects. Understanding the role of Prolyl 3-hydroxylase 1 in collagen biosynthesis and its mutations could pave the way for novel therapeutic strategies targeting bone disorders and improving patient outcomes.