Explore the Potential with AI-Driven Innovation
This comprehensive focused library is produced on demand with state-of-the-art virtual screening and parameter assessment technology driven by Receptor.AI drug discovery platform. This approach outperforms traditional methods and provides higher-quality compounds with superior 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 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 top-notch dedicated system is used to design specialised libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The method includes detailed molecular simulations of the catalytic and allosteric binding pockets, along with ensemble virtual screening that considers their conformational flexibility. In the design of modulators, structural changes induced by reaction intermediates are taken into account to enhance activity and selectivity.
Key features that set our library apart include:
partner
Reaxense
upacc
Q96PP8
UPID:
GBP5_HUMAN
Alternative names:
GBP-TA antigen; GTP-binding protein 5; Guanine nucleotide-binding protein 5
Alternative UPACC:
Q96PP8; B2RCE1; Q86TM5
Background:
Guanylate-binding protein 5 (GBP5) is a pivotal player in the innate immune response, characterized by its unique ability to hydrolyze GTP without producing GMP. Unlike other family members, GBP5 is specifically recruited to pathogen-containing vacuoles or vacuole-escaped bacteria, enhancing the assembly of inflammasomes. It facilitates the lysis of these vacuoles, releasing pathogens into the cytosol and thereby promoting the recruitment of bacterial cytolysis mediators. This process liberates ligands detected by inflammasomes, crucial for activating the non-canonical CASP4/CASP11 and AIM2 inflammasomes, and selectively assembles the NLRP3 inflammasome in response to microbial agents.
Therapeutic significance:
Understanding the role of Guanylate-binding protein 5 could open doors to potential therapeutic strategies, particularly in enhancing innate immune responses and inflammasome assembly for combating bacterial, viral, and protozoan pathogens.