Structure of the adenosine A(2A) receptor in complex with ZM241385 and the xanthines XAC and caffeine.

Abstract in brief

• The study presents the crystal structures of the adenosine A2A receptor in complex with various ligands, including xanthines like caffeine, XAC, and the inverse agonist ZM241385, revealing its inactive state with a specific salt bridge called the ionic lock.
• These structures offer new understanding of how different ligands bind within the receptor's pocket and highlight the receptor’s intracellular regions involved in signal transduction, which is important for developing drugs to treat conditions like Parkinson's disease.
• Methylxanthines such as caffeine are common stimulants that work by blocking adenosine receptors, and the detailed structural data can help improve their therapeutic properties or develop new treatments for neurological diseases.]