Fig. 1: Fluorescence reporter design to detect clamshell motions of iGluR LBDs. | Communications Biology

Fig. 1: Fluorescence reporter design to detect clamshell motions of iGluR LBDs.

From: Allosteric coupling of sub-millisecond clamshell motions in ionotropic glutamate receptor ligand-binding domains

Fig. 1

a Structural architecture of iGluRs and expanded view on the LBD, including the PET fluorescence reporter design for clamshell motions. In the bi-lobate LBD clamshell structure, the engineered Cys (red sticks) modified with fluorophore (orange sphere), and the engineered Trp (blue sticks) at the mouth of the clamshell, detect conformational dynamics (gray arrow) through contact-induced fluorescence quenching. The bound agonist is shown as yellow spheres and the upper D1 and lower D2 lobe is indicated. b–d Crystal structures of agonist-bound GluA2 (b), GluK1 (c), and GluN1 (d) LBDs in comic representation (PDB IDs: 2UXA, 1TXF, and 1PB7; for GluA2, GluK1, and GluN1, respectively). The structures are oriented as shown on the right-hand side of panel (a). Sites for fluorescence modification (engineered Cys) are shown as red sticks. Engineered Trp residues are shown as blue sticks. The bound agonist is highlighted as yellow spheres.

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