Focused On-demand Library for Calcium-binding and coiled-coil domain-containing protein 2

Available from Reaxense
Predicted by Alphafold

Focused On-demand Libraries - Reaxense Collaboration

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 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 promising modulators annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Also, each compound is presented with its optimal docking poses, affinity scores, and activity scores, providing a comprehensive overview.

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.

Our library is unique due to several crucial aspects:

  • Receptor.AI compiles all relevant data on the target protein, such as past experimental results, literature findings, known ligands, and structural data, thereby enhancing the likelihood of focusing on the most significant compounds.
  • By utilizing advanced molecular simulations, the platform is adept at locating potential binding sites, rendering the compounds in the focused library well-suited for unearthing allosteric inhibitors and binders for hidden pockets.
  • The platform is supported by more than 50 highly specialized AI models, all of which have been rigorously tested and validated in diverse drug discovery and research programs. Its design emphasizes efficiency, reliability, and accuracy, crucial for producing focused libraries.
  • Receptor.AI extends beyond just creating focused libraries; it offers a complete spectrum of services and solutions during the preclinical drug discovery phase, with a success-dependent pricing strategy that reduces risk and fosters shared success in the project.







Alternative names:

Antigen nuclear dot 52 kDa protein; Nuclear domain 10 protein NDP52; Nuclear dot protein 52

Alternative UPACC:

Q13137; B2RBT0; B4DDC4; B4DDT4; B4DP36; B4E0C0; E7ENK0; E7ETP5; E9PBE5; Q53FQ5; Q53HB5; Q6IBN9; Q9BTF7


Calcium-binding and coiled-coil domain-containing protein 2, also known as Nuclear domain 10 protein NDP52, plays a pivotal role in autophagy, specifically targeting intracellular bacteria like Salmonella typhimurium for degradation. It acts as an effector in galectin-sensed membrane damage, orchestrating the targeting of bacteria to autophagosomes and ensuring their degradation by regulating autophagosome maturation. Its interaction with MAP1LC3A, MAP1LC3B, GABARAPL2, and MAP3LC3C is crucial for these processes. Additionally, NDP52 may influence actin cytoskeleton organization and negatively regulate constitutive secretion.

Therapeutic significance:

Understanding the role of Calcium-binding and coiled-coil domain-containing protein 2 could open doors to potential therapeutic strategies.

Looking for more information on this library or underlying technology? Fill out the form below and we'll be in touch with all the details you need.
Thank you! Your submission has been received!
Oops! Something went wrong while submitting the form.