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.
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 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.
We utilise our cutting-edge, exclusive workflow to develop focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology leverages molecular simulations to examine a vast array of proteins, capturing their dynamics in both isolated forms and in complexes with other proteins. Through ensemble virtual screening, we thoroughly account for the protein's conformational mobility, identifying critical binding sites within functional regions and distant allosteric locations. This detailed exploration ensures that we comprehensively assess every possible mechanism of action, with the objective of identifying novel therapeutic targets and lead compounds that span a wide spectrum of biological functions.
Several key aspects differentiate our library:
partner
Reaxense
upacc
Q4FZB7
UPID:
KMT5B_HUMAN
Alternative names:
Lysine N-methyltransferase 5B; Lysine-specific methyltransferase 5B; Suppressor of variegation 4-20 homolog 1; [histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B; [histone H4]-lysine20 N-methyltransferase KMT5B
Alternative UPACC:
Q4FZB7; A0A0A0MT19; B7WNX7; Q3SX56; Q4V775; Q6P150; Q96E44; Q9BUL0; Q9H022; Q9H2K3; Q9NXV3; Q9Y393
Background:
Histone-lysine N-methyltransferase KMT5B, also known as Lysine N-methyltransferase 5B, plays a pivotal role in chromatin structure and function by specifically methylating histone H4 on Lys-20. This methylation is crucial for transcription regulation and maintaining genome integrity. KMT5B's activity contributes to the formation of constitutive heterochromatin in pericentric regions and is essential in myogenesis and DNA repair processes.
Therapeutic significance:
KMT5B's mutation is linked to Intellectual developmental disorder, autosomal dominant 51, highlighting its critical role in cognitive function. Understanding KMT5B's mechanisms could lead to novel therapeutic strategies for treating intellectual developmental disorders and enhancing DNA repair in genetic diseases.