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.
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.
In the library, a selection of top modulators is provided, each marked with 38 ADME-Tox and 32 parameters related to physicochemical properties and drug-likeness. Also, every compound comes with its best docking poses, affinity scores, and activity scores, providing a comprehensive overview.
We employ our advanced, specialised process to create targeted libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our strategy employs molecular simulations to explore an extensive range of proteins, capturing their dynamics both individually and within complexes with other proteins. Through ensemble virtual screening, we address proteins' conformational mobility, uncovering key binding sites at both functional regions and remote allosteric locations. This comprehensive investigation ensures a thorough assessment of all potential mechanisms of action, with the goal of discovering innovative therapeutic targets and lead molecules across across diverse biological functions.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q86UT6
UPID:
NLRX1_HUMAN
Alternative names:
Caterpiller protein 11.3; Nucleotide-binding oligomerization domain protein 5; Nucleotide-binding oligomerization domain protein 9
Alternative UPACC:
Q86UT6; A8K6Q1; B3KPK2; B3KTA2; Q7RTR3; Q96D51; Q9H724
Background:
NLR family member X1, also known as Caterpiller protein 11.3, Nucleotide-binding oligomerization domain protein 5, and Nucleotide-binding oligomerization domain protein 9, plays a crucial role in antiviral signaling. It acts as a negative regulator of MAVS-mediated antiviral responses and promotes autophagy by interacting with TUFM. Additionally, it regulates MAVS-dependent NLRP3 inflammasome activation to attenuate apoptosis and enhances NF-kappa-B and JUN N-terminal kinase dependent signaling.
Therapeutic significance:
Understanding the role of NLR family member X1 could open doors to potential therapeutic strategies, particularly in modulating antiviral responses and autophagy processes.