Abstract
A major goal in molecular neuroscience is to understand structure-function relationships of glutamate receptor ion channels (iGluRs) and their role in behavior. In the mammalian central nervous system, iGluRs form non-selective cation channels that generate depolarizing potentials in fast excitatory synaptic processes. Having earlier introduced the light-activated glutamate receptor LiGuR, we went one step further and applied two types of structure-based design to develop a potassium selective, light-gated ion channel. Simple and fast Monte-Carlo simulations allow the rational design of optically-controlled proteins in general and LiGluR variants in particular. Using homology modeling we modified the transmembrane pore-region of LiGluR to create a potassium selective channel that responds to glutamate and light. We demonstrate that rapid pulses of light can hyperpolarize HEK-293 cells and neurons expressing this novel channel, which can be used as a tool in glutamate receptor screening applications and may enable optical neuronal inhibition.
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