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.
Our selection of compounds is from a large virtual library of over 60 billion molecules. The production and distribution of these compounds are managed by our partner Reaxense.
The library features a range of promising modulators, each detailed with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Plus, each compound is presented with its ideal docking poses, affinity scores, and activity scores, ensuring a thorough insight.
We employ our advanced, specialised process to create targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
It includes in-depth molecular simulations of both the catalytic and allosteric binding pockets, with ensemble virtual screening focusing on their conformational flexibility. For modulators, the process includes considering the structural shifts due to reaction intermediates to boost activity and selectivity.
Key features that set our library apart include:
partner
Reaxense
upacc
P98194
UPID:
AT2C1_HUMAN
Alternative names:
ATP-dependent Ca(2+) pump PMR1; Ca(2+)/Mn(2+)-ATPase 2C1; Secretory pathway Ca(2+)-transporting ATPase type 1
Alternative UPACC:
P98194; B2RAT7; B4DSW3; B7Z3X9; G3XAH8; G8JLN9; O76005; Q86V72; Q86V73; Q8N6V1; Q8NCJ7
Background:
Calcium-transporting ATPase type 2C member 1, also known as ATP-dependent Ca(2+) pump PMR1, plays a crucial role in maintaining Ca(2+) homeostasis in the trans-Golgi compartment. It functions by transporting Ca(2+) and Mn(2+) ions from the cytoplasm to the lumen of the Golgi apparatus, a process essential for the proper sorting and trafficking of newly synthesized proteins. This protein's activity is pivotal in keratinocyte differentiation, epidermis integrity, and neural polarity.
Therapeutic significance:
Mutations in this protein are linked to Hailey-Hailey disease, an autosomal dominant disorder characterized by blistering skin due to impaired keratinocyte adhesion. Understanding the role of Calcium-transporting ATPase type 2C member 1 could lead to targeted therapies for this debilitating condition.