The results revealed a clear trend: in the F601D-ADGRG2 system, polar amino acids such as Y758 ECL2 , K760 ECL2 , N775 5.32 , and N860 7.46 primarily stabilize the inactive state of ADGRG2, whereas hydrophobic residues like L693 3.36 , L697 3.44 and F769 ECL2 promote the receptor’s active state( Figure 7 A,D).
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Exploring the Binding Mechanism of ADGRG2 Through Metadynamics and Biochemical Analysis.
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