Fig. 5: Reconstitution and characterization of mGluR7 in native NDs.
From: DeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides
a Illustration of the mGluR7-ELFN complex at neuronal synapses. mGluR7 is a prominent metabotropic glutamate receptor that modulates synaptic transmission. Recent studies demonstrate that its function is also regulated by trans-synaptic interactions with ELFN-162. b Representative clear native gel of mGluR7 in Hex20B1WA NDs binding to ELFN-1. Native NDs harboring mGLuR7 were incubated with increasing concentrations of the extracellular fragment of ELFN-1. Samples were analyzed by native electrophoresis and in-gel fluorescence imaging. c Quantification of mGluR7 interaction with ELFN-1 from native gel analysis as described in (b). The decreased densities of the mGluR7 band normalized to the protein alone (lane 1) was used to calculate the relative binding to ELFN-1 at various concentrations. The binding data of mGluR7 with ELFN-1 was then fitted with the Hill equation (Kd = 8 ± 1 µM; n = 2.6). Data are shown as mean ± s.d., n  =  3 independent experiments.
