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.
The compounds are cherry-picked from the vast virtual chemical space of over 60B molecules. The synthesis and delivery of compounds is facilitated by our partner Reaxense.
The library includes a list of the most effective modulators, each annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Furthermore, each compound is shown with its optimal docking poses, affinity scores, and activity scores, offering a detailed summary.
We employ our advanced, specialised process to create targeted 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 stands out due to several important features:
partner
Reaxense
upacc
Q8WTX7
UPID:
CAST1_HUMAN
Alternative names:
Cellular arginine sensor for mTORC1 protein 1; GATS-like protein 3
Alternative UPACC:
Q8WTX7; O76052; Q96ND9; Q9UIE8
Background:
Cytosolic arginine sensor for mTORC1 subunit 1 (CASTOR1) plays a pivotal role in the amino acid-sensing branch of the TORC1 signaling pathway. As a homodimer or heterodimer with CASTOR2, it regulates mTORC1 by binding and inhibiting the GATOR2 subcomplex. The interaction with arginine allosterically disrupts its binding to GATOR2, activating mTORC1.
Therapeutic significance:
Understanding the role of Cytosolic arginine sensor for mTORC1 subunit 1 could open doors to potential therapeutic strategies.