Explore the Potential with AI-Driven Innovation
The focused library is created on demand with the latest virtual screening and parameter assessment technology, supported by the Receptor.AI drug discovery platform. This method is more effective than traditional methods and results in higher-quality compounds with better 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 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.
Our top-notch dedicated system is used to design specialised libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology employs molecular simulations to explore a wide array of proteins, capturing their dynamic states both individually and within complexes. Through ensemble virtual screening, we address conformational mobility, uncovering binding sites within functional regions and remote allosteric locations. This thorough exploration ensures no potential mechanism of action is overlooked, aiming to discover novel therapeutic targets and lead compounds across an extensive spectrum of biological functions.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
P52294
UPID:
IMA5_HUMAN
Alternative names:
Karyopherin subunit alpha-1; Nucleoprotein interactor 1; RAG cohort protein 2; SRP1-beta
Alternative UPACC:
P52294; D3DN93; Q6IBQ9; Q9BQ56
Background:
Importin subunit alpha-5, also known as Karyopherin subunit alpha-1, plays a crucial role in nuclear protein import. It functions as an adapter for nuclear receptor KPNB1, binding directly to substrates with NLS motifs. This protein is essential for the translocation of importin/substrate complexes through the nuclear pore complex, facilitated by KPNB1's interaction with nucleoporin FxFG repeats. The process is powered by Ran-dependent mechanisms, ensuring the directionality of nuclear import through the asymmetric distribution of Ran's GTP- and GDP-bound forms.
Therapeutic significance:
Understanding the role of Importin subunit alpha-5 could open doors to potential therapeutic strategies.