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 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.
We use our state-of-the-art dedicated workflow for designing focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Utilising molecular simulations, our approach thoroughly examines a wide array of proteins, tracking their conformational changes individually and within complexes. Ensemble virtual screening enables us to address conformational flexibility, revealing essential binding sites at functional regions and allosteric locations. Our rigorous analysis guarantees that no potential mechanism of action is overlooked, aiming to uncover new therapeutic targets and lead compounds across diverse biological functions.
Key features that set our library apart include:
partner
Reaxense
upacc
P68431
UPID:
H31_HUMAN
Alternative names:
Histone H3/a; Histone H3/b; Histone H3/c; Histone H3/d; Histone H3/f; Histone H3/h; Histone H3/i; Histone H3/j; Histone H3/k; Histone H3/l
Alternative UPACC:
P68431; A0PJT7; A5PLR1; P02295; P02296; P16106; Q6ISV8; Q6NWP8; Q6NWP9; Q6NXU4; Q71DJ3; Q93081
Background:
Histone H3.1, encoded by the gene with accession number P68431, is a core component of the nucleosome, essential for wrapping and compacting DNA into chromatin. This process is crucial for transcription regulation, DNA repair, replication, and chromosomal stability. Histone H3.1 undergoes various post-translational modifications, contributing to the histone code that regulates DNA accessibility.
Therapeutic significance:
Mutations in Histone H3.1, particularly affecting residue Lys-28, have been linked to the pathogenesis of aggressive gliomas, including pediatric glioblastoma and diffuse intrinsic pontine glioma. These mutations alter histone methylation, disrupt Polycomb repressive complex 2 activity, and lead to aberrant gene expression, highlighting the protein's potential as a target for therapeutic intervention.