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.
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.
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.
Key features that set our library apart include:
partner
Reaxense
upacc
Q86VP6
UPID:
CAND1_HUMAN
Alternative names:
Cullin-associated and neddylation-dissociated protein 1; TBP-interacting protein of 120 kDa A; p120 CAND1
Alternative UPACC:
Q86VP6; B2RAU3; O94918; Q6PIY4; Q8NDJ4; Q96JZ9; Q96T19; Q9BTC4; Q9H0G2; Q9P0H7; Q9UF85
Background:
Cullin-associated NEDD8-dissociated protein 1 (CAND1) is a pivotal component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, facilitating the exchange of F-box subunits. This process is crucial for the dynamic regulation of protein degradation, a fundamental cellular mechanism. CAND1's activity is intricately linked with neddylation cycles, influencing the assembly and function of cullin-RING E3 ligases.
Therapeutic significance:
Understanding the role of Cullin-associated NEDD8-dissociated protein 1 could open doors to potential therapeutic strategies.