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 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.
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 utilise our cutting-edge, exclusive workflow to develop focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our strategy employs molecular simulations to explore an extensive range of proteins, capturing their dynamics both individually and within complexes with other proteins. Through ensemble virtual screening, we address proteins' conformational mobility, uncovering key binding sites at both functional regions and remote allosteric locations. This comprehensive investigation ensures a thorough assessment of all potential mechanisms of action, with the goal of discovering innovative therapeutic targets and lead molecules across across diverse biological functions.
Several key aspects differentiate our library:
partner
Reaxense
upacc
Q15006
UPID:
EMC2_HUMAN
Alternative names:
Tetratricopeptide repeat protein 35
Alternative UPACC:
Q15006; Q8WUE1
Background:
ER membrane protein complex subunit 2, also known as Tetratricopeptide repeat protein 35, plays a crucial role in the endoplasmic reticulum membrane protein complex (EMC). It facilitates the energy-independent insertion of newly synthesized membrane proteins into endoplasmic reticulum membranes. This protein is adept at accommodating proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features. It is essential for the cotranslational and post-translational insertion of multi-pass and tail-anchored proteins into the ER membrane, influencing the topology of multi-pass membrane proteins like G protein-coupled receptors.
Therapeutic significance:
Understanding the role of ER membrane protein complex subunit 2 could open doors to potential therapeutic strategies.