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doi: 10.1039/D4SU00448E 117 PathakJ.SinghP

Since GluK5 binds Glu with higher affinity and favors slower deactivation kinetics compared to GluK2, the GluK2/K5 heterotetramer can be activated by the ligand that binds to GluK5 subunits only, without binding to GluK2 subunits ( FIGURE 8 Along with the agonist-bound structure characterized by four-fold symmetrical LBD layer, a recent study of GluK2 revealed a Glu-bound structure, where one LBD dimer was preserved, while the other LBD dimer dissociated through 100 rotation of one protomer relative to the other (Figure 8B) (Gangwar et al., 2024b), similar to that observed in the putative apo state mentioned above (Figure 4C)

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