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 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.
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.
Our top-notch dedicated system is used to design specialised libraries.
Fig. 1. The sreening workflow of Receptor.AI
By deploying molecular simulations, our approach comprehensively covers a broad array of proteins, tracking their flexibility and dynamics individually and within complexes. Ensemble virtual screening is utilised to take into account conformational dynamics, identifying pivotal binding sites located within functional regions and at allosteric locations. This thorough exploration ensures that every conceivable mechanism of action is considered, aiming to identify new therapeutic targets and advance lead compounds throughout a vast spectrum of biological functions.
Several key aspects differentiate our library:
partner
Reaxense
upacc
O00629
UPID:
IMA3_HUMAN
Alternative names:
Importin alpha Q1; Karyopherin subunit alpha-4
Alternative UPACC:
O00629; A8K4S6; D3DNM2; O00190
Background:
Importin subunit alpha-3, also known as Importin alpha Q1 and Karyopherin subunit alpha-4, plays a crucial role in nuclear protein import. It functions as an adapter protein for nuclear receptor KPNB1, binding directly to substrates with NLS motifs. This protein is essential for the docking of the importin/substrate complex to the nuclear pore complex, facilitated by KPNB1's interaction with nucleoporin FxFG repeats. The complex's translocation through the pore relies on a Ran-dependent mechanism, with the directionality of nuclear import influenced by the distribution of GTP- and GDP-bound forms of Ran.
Therapeutic significance:
Understanding the role of Importin subunit alpha-3 could open doors to potential therapeutic strategies.