Explore the Potential with AI-Driven Innovation
The specialised, focused library is developed on demand with the most recent virtual screening and parameter assessment technology, guided by the Receptor.AI drug discovery platform. This approach exceeds the capabilities of traditional methods and offers compounds with higher activity, selectivity, and safety.
Our selection of compounds is from a large virtual library of over 60 billion molecules. The production and distribution of these compounds are managed 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
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
P01834
UPID:
IGKC_HUMAN
Alternative names:
Ig kappa chain C region; Ig kappa chain C region AG; Ig kappa chain C region CUM; Ig kappa chain C region EU; Ig kappa chain C region OU; Ig kappa chain C region ROY; Ig kappa chain C region TI
Alternative UPACC:
P01834; A0A075B6H6; A0A087X130
Background:
The Immunoglobulin kappa constant plays a pivotal role in the immune response. It is part of the immunoglobulin light chains, crucial for the formation of antibodies by B lymphocytes. These antibodies are essential for recognizing and eliminating antigens, with the kappa constant region contributing to the antibody's stability and specificity. The protein is encoded by a gene that, when mutated, leads to Immunoglobulin kappa light chain deficiency, a condition marked by the absence of kappa chains.
Therapeutic significance:
Given its fundamental role in humoral immunity, targeting the Immunoglobulin kappa constant could offer novel therapeutic avenues for treating Immunoglobulin kappa light chain deficiency. Enhancing our understanding of this protein's function and its interaction with antigens could pave the way for innovative treatments.