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.
Contained in the library are leading modulators, each labelled with 38 ADME-Tox and 32 physicochemical and drug-likeness qualities. In addition, each compound is illustrated with its optimal docking poses, affinity scores, and activity scores, giving a complete picture.
Our top-notch dedicated system is used to design specialised 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.
Key features that set our library apart include:
partner
Reaxense
upacc
P01871
UPID:
IGHM_HUMAN
Alternative names:
Ig mu chain C region; Ig mu chain C region BOT; Ig mu chain C region GAL; Ig mu chain C region OU
Alternative UPACC:
P01871; A0A075B6N9; A0A0G2JQL4; P04220; P20769
Background:
The Immunoglobulin heavy constant mu (IgM) plays a pivotal role in the immune system as a primary defender against pathogens. It is a key component of the humoral immune response, facilitating the recognition and elimination of antigens through its unique antigen-binding sites. IgM's structure allows for the assembly of its variable domains through V-(D)-J rearrangement, enabling somatic hypermutations for affinity maturation against specific antigens.
Therapeutic significance:
Agammaglobulinemia 1, an autosomal recessive disorder, underscores the critical role of IgM in immune defense. This condition, characterized by low or absent serum antibodies and B cells, highlights the potential of targeting IgM pathways for therapeutic interventions to restore immune function and prevent severe infections.