CALIXAR’s Adenosine receptor A2A facilitates reliable fragment-based drug design (FBDD), structure-based drug discovery (SBDD) and antibody discovery corresponding to this specific target.
Unlike CALIXAR’s Adenosine receptor A2A, other alternative methods result in an adenosine receptor that becomes mutated and truncated (96 amino-acids truncation in the C-terminus). Additionally, this mutated version becomes locked within an antagonist conformation.
As with all GPCRs, the Adenosine receptor A2A is an unstable target and is difficult to produce natively with conventional approaches. Previously, Adenosine receptor A2A could only be locked in one specific conformation (e.g. antagonist) and were only ever prepared in a solution that inherently could not be pure, nor native (truncated, mutated) and without PTMs. A2AR’s have only ever been inherently unstable, but not anymore.
Today, CALIXAR’s Adenosine receptor A2A is able to bind to agonists, antagonists, as well as allosteric modulators (Igonet S. et al., 2018, Scientific Reports). Our Adenosine receptor A2A also maintain its structural and functional integrity and is purified and stabilized to full length and wild-type (native) proteins.
- Antibodies (including nanobodies, scaffold proteins, aptamers)
- Small molecules
- 3D Structures (classical X-ray or XFEL, Cryo-EM, NMR)
- Drug discovery (Screening: HTS, FBDD, SBDD; Hit and lead validation)
- Antibody discovery (Immunization and display technologies)
- Clinical stage (drug validation on reliable native A2A)