A method for identifying G protein-coupled receptor dimers and their interfaces

The G protein-coupled receptor (GPCR) dimer interface plays an important role in the formation and stabilization of dimer. Therefore, identifying potential receptor-receptor is part studying GPCRs. Various strategies have been employed to study GPCR explore its functional significance, but experimental methods lack robustness calculations are laborious. Herein, we report a combined optimized calculation approach for structurally characterizing interfaces, constructing atomic resolution models. Using transmembrane domain (TM) peptide containing human immunodeficiency virus trans-acting transcriptional activator (HIV-TAT) protein transduction motif, matrix-assisted laser desorption tandem time-of-flight mass spectrometry (MALDITOF-MS), bioluminescence resonance energy transfer (BRET), successfully identified Apelin (APJ)/Nociceptin 1 (ORL1) APJ/Vasopressin 2 (V2R) heterodimer two key sites mediating dimerization. This method can identify interfaces homodimers heterodimers.