Explore the Potential with AI-Driven Innovation
This extensive focused library is tailor-made using the latest virtual screening and parameter assessment technology, operated by the Receptor.AI drug discovery platform. This technique is more effective than traditional methods, offering compounds with improved 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.
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 use our state-of-the-art dedicated workflow for designing focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology leverages molecular simulations to examine a vast array of proteins, capturing their dynamics in both isolated forms and in complexes with other proteins. Through ensemble virtual screening, we thoroughly account for the protein's conformational mobility, identifying critical binding sites within functional regions and distant allosteric locations. This detailed exploration ensures that we comprehensively assess every possible mechanism of action, with the objective of identifying novel therapeutic targets and lead compounds that span a wide spectrum of biological functions.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q9P0I2
UPID:
EMC3_HUMAN
Alternative names:
Transmembrane protein 111
Alternative UPACC:
Q9P0I2; B2R4Z9; Q53GH8; Q6ZMC2
Background:
ER membrane protein complex subunit 3, also known as Transmembrane protein 111, is integral to the endoplasmic reticulum membrane protein complex (EMC). It plays a pivotal role in the insertion of newly synthesized membrane proteins into the endoplasmic reticulum membranes, accommodating proteins with transmembrane domains that are weakly hydrophobic. This protein is crucial for the cotranslational insertion of multi-pass membrane proteins and the post-translational insertion of tail-anchored proteins, influencing the topology of multi-pass membrane proteins like G protein-coupled receptors.
Therapeutic significance:
Understanding the role of ER membrane protein complex subunit 3 could open doors to potential therapeutic strategies.