Explore the Potential with AI-Driven Innovation
This comprehensive focused library is produced on demand with state-of-the-art virtual screening and parameter assessment technology driven by Receptor.AI drug discovery platform. This approach outperforms traditional methods and provides higher-quality compounds with superior 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.
Our top-notch dedicated system is used to design specialised libraries.
Fig. 1. The sreening workflow of Receptor.AI
Utilising molecular simulations, our approach thoroughly examines a wide array of proteins, tracking their conformational changes individually and within complexes. Ensemble virtual screening enables us to address conformational flexibility, revealing essential binding sites at functional regions and allosteric locations. Our rigorous analysis guarantees that no potential mechanism of action is overlooked, aiming to uncover new therapeutic targets and lead compounds across diverse biological functions.
Our library stands out due to several important features:
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.