Explore the Potential with AI-Driven Innovation
This extensive focused library is tailor-made using the latest virtual screening and parameter assessment technology, operated by the Receptor.AI drug discovery platform. This technique is more effective than traditional methods, offering compounds with improved activity, selectivity, and safety.
We carefully select specific compounds from a vast collection of over 60 billion molecules in virtual chemical space. Our partner Reaxense helps in synthesizing and delivering these compounds.
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.
Our high-tech, dedicated method is applied to construct targeted libraries.
Fig. 1. The sreening workflow of Receptor.AI
By deploying molecular simulations, our approach comprehensively covers a broad array of proteins, tracking their flexibility and dynamics individually and within complexes. Ensemble virtual screening is utilised to take into account conformational dynamics, identifying pivotal binding sites located within functional regions and at allosteric locations. This thorough exploration ensures that every conceivable mechanism of action is considered, aiming to identify new therapeutic targets and advance lead compounds throughout a vast spectrum of biological functions.
Our library distinguishes itself through several key aspects:
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.