CALIXAR’s A2A Adenosine receptors facilitate reliable fragment-based drug design (FBDD), structure-based drug discovery (SBDD) and antibody discovery corresponding to this specific target. 

Unlike CALIXAR’s A2A Adenosine receptors, 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 A2A Adenosine receptor is an unstable target and is difficult to produce natively with conventional approaches. Previously, A2A Adenosine receptors 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. A2A’s have only ever been inherently unstable, but not anymore.

Today, CALIXAR’s A2A receptors are able to bind to agonists, antagonists, as well as allosteric modulators (Igonet S. et al., 2018, Scientific Reports). Our A2A receptors also maintain their structural and functional integrity and are purified and stabilized to full length and wild-type (native) proteins.