Explore the Potential with AI-Driven Innovation
Our detailed focused library is generated on demand with advanced virtual screening and parameter assessment technology powered by the Receptor.AI drug discovery platform. This method surpasses traditional approaches, delivering compounds of better quality with enhanced 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 promising modulators annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Also, each compound is presented with its optimal docking poses, affinity scores, and activity scores, providing a comprehensive overview.
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 is unique due to several crucial aspects:
partner
Reaxense
upacc
O75190
UPID:
DNJB6_HUMAN
Alternative names:
HHDJ1; Heat shock protein J2; MRJ; MSJ-1
Alternative UPACC:
O75190; A4D232; A8K7D8; A8KAG0; B4DN73; E9PCZ2; O95806; Q53EN8; Q59EF2; Q6FIC8; Q75MA2; Q9UIK6
Background:
DnaJ homolog subfamily B member 6, known by alternative names such as HHDJ1, Heat shock protein J2, MRJ, and MSJ-1, plays a crucial role in cellular processes. It enhances the ATPase activity of HSP70, acting as a co-chaperone. This protein is vital in organizing KRT8/KRT18 filaments and serves as a molecular chaperone for neuronal proteins, including huntingtin, reducing aggregation and toxicity of polyglutamine-containing proteins.
Therapeutic significance:
Linked to Muscular dystrophy, limb-girdle, autosomal dominant 1, DnaJ homolog subfamily B member 6's dysfunction, particularly isoform B, is implicated in disease pathogenesis. Understanding its role could lead to novel therapeutic strategies for this and related myopathies.