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.
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 utilise our cutting-edge, exclusive workflow to develop focused libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The method includes detailed molecular simulations of the catalytic and allosteric binding pockets, along with ensemble virtual screening that considers their conformational flexibility. In the design of modulators, structural changes induced by reaction intermediates are taken into account to enhance activity and selectivity.
Several key aspects differentiate our library:
partner
Reaxense
upacc
P38935
UPID:
SMBP2_HUMAN
Alternative names:
ATP-dependent helicase IGHMBP2; Glial factor 1; Immunoglobulin mu-binding protein 2
Alternative UPACC:
P38935; A0PJD2; Q00443; Q14177
Background:
DNA-binding protein SMUBP-2, also known as ATP-dependent helicase IGHMBP2, plays a crucial role in unwinding RNA and DNA duplexes in an ATP-dependent manner. It specifically targets 5'-phosphorylated single-stranded guanine-rich sequences, indicating a specialized function in nucleic acid metabolism. This protein is implicated in various cellular processes including RNA metabolism, ribosome biogenesis, and potentially in the initiation of translation and regulation of transcription.
Therapeutic significance:
DNA-binding protein SMUBP-2 is linked to two significant neuromuscular disorders: Neuronopathy, distal hereditary motor, 6, and Charcot-Marie-Tooth disease, axonal, 2S. Both diseases are characterized by progressive muscle weakness and atrophy, attributed to mutations affecting the gene encoding this protein. Understanding the role of DNA-binding protein SMUBP-2 could open doors to potential therapeutic strategies for these debilitating conditions.