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.
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 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 high-tech, dedicated method is applied to construct targeted 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
P25686
UPID:
DNJB2_HUMAN
Alternative names:
Heat shock 40 kDa protein 3; Heat shock protein J1
Alternative UPACC:
P25686; A8K9P6; Q53QD7; Q8IUK1; Q8IUK2; Q96F52
Background:
DnaJ homolog subfamily B member 2, also known as Heat shock 40 kDa protein 3 or Heat shock protein J1, plays a pivotal role in cellular stress responses. It functions as a co-chaperone, enhancing the ATPase activity of HSP70 family chaperones, crucial for protein folding and repair. Additionally, it aids in the proteasomal degradation of misfolded proteins, preventing their aggregation and promoting cellular recovery.
Therapeutic significance:
The protein is linked to Distal spinal muscular atrophy, autosomal recessive, 5, a neurologic disorder characterized by muscle weakness and atrophy. Understanding the role of DnaJ homolog subfamily B member 2 in this condition could pave the way for novel therapeutic strategies targeting motor nerve function and protein homeostasis.