Crystal structure of the adenosine A_2A receptor bound to an antagonist reveals a potential allosteric pocket.

ABSTRACT: The adenosine A_2A receptor (A_2AR) has long been implicated in cardiovascular disorders. As more selective A_2AR ligands are being identified, its roles in other disorders, such as Parkinson's disease, are starting to emerge, and A_2AR antagonists are important drug candidates for nondopaminergic anti-Parkinson treatment. Here we report the crystal structure of A_2A receptor bound to compound 1 (Cmpd-1), a novel A_2AR/N-methyl d-aspartate receptor subtype 2B (NR2B) dual antagonist and potential anti-Parkinson candidate compound, at 3.5 Å resolution. The A_2A receptor with a cytochrome b562-RIL (BRIL) fusion (A_2AR-BRIL) in the intracellular loop 3 (ICL3) was crystallized in detergent micelles using vapo

SUBMITTER: Sun B 

PROVIDER: S-EPMC5338372 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature