Abstract
AbstractG‐protein‐coupled‐receptors (GPCRs) are of fundamental importance for signal transduction through cell membranes. This makes them important drug targets, but structure‐based drug design (SBDD) is still hampered by the limitations for structure determination of unmodified GPCRs. We show that the interligand NOEs for pharmacophore mapping (INPHARMA) method can provide valuable information on ligand poses inside the binding site of the unmodified human A2A adenosine receptor reconstituted in nanodiscs. By comparing experimental INPHARMA spectra with back‐calculated spectra based on ligand poses obtained from molecular dynamics simulations, a complex structure for A2AR with the low‐affinity ligand 3‐pyrrolidin‐1‐ylquinoxalin‐2‐amine was determined based on the X‐ray structure of ligand ZM‐241,358 in complex with a modified A2AR.
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