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• W2934526315 abstract "Ionotropic glutamate receptors form the basic structures for rapid excitatory signal transmission in the central nervous system. After the binding of a ligand and the resulting pore opening, they allow an ion flow across the membrane. From an evolutionary point of view, these are highly developed and highly complex structures composed of different domains. There is a ligand binding domain necessary for ligand recognition coupled to the pore which is responsible for the real ion conduction. Extracellular additionally the n-terminal domain and intracellular the c-terminal is located both involved in modulational tasks where the n-terminus should also be responsible for the assembly.Due to the structural similarity and overlaps in the sequence, it has been assumed for years that these highly engineered receptors originally evolved through a fusion of substrate binding proteins and upturned potassium channels. However, attempting to rebuild a glutamate receptor to a potassium selective one or even to install a potassium channel failed. GluR0, a bacterial glutamate receptor, shows an increased potassium selectivity what is a further indication for this theory but could not be merged with mammalian receptor so far.In the first chapter I can show that it is possible to insert a rudimentary potassium channel (KcvATCV-1) in an inverted orientation into the cell membrane. This property fits perfect to the idea to exchange the pore of a glutamate receptor to make it potassium selective. In the second chapter I designed a chimera out of a KcvATCV-1 and a highly developed glutamate receptor (GluA1). Using this chimera, I demonstrated that it is possible to gate a potassium channel by the gating machinery of a glutamate receptor. In this chimeric receptor the most important pharmacological parameters of the GluA1 are obtained even though the selectivity of the KcvATCV-1 is transferred. The studied main characteristics of the potassium channel, the barium block and also the selectivity are still present as well as the effects of certain mutations on channel behavior. In turn, the chimera still reacts to the same agonists and antagonists as the origin receptor. Interestingly, not even the apparent affinity for the tested agonists and antagonists was affected in the chimeric receptor. In the third chapter, a connection to the bacterial GluR0 could be opened. Mammalian wild-type receptors, unlike GluR0, possess an essential extra transmembrane domain. Removing of this extra transmembrane domain in mammalian receptors makes them unfunctional. Interestingly this third TM can be removed in the chimera. A function, albeit with a reduced affinity for glutamate, is still present." @default.
• W2934526315 created "2019-04-11" @default.
• W2934526315 creator A5006509181 @default.
• W2934526315 date "2019-01-01" @default.
• W2934526315 modified "2023-09-27" @default.
• W2934526315 title "Modular design of ionotropic glutamate receptors: Coupling of a viral K+-channel with a glutamate-binding domain" @default.
• W2934526315 hasPublicationYear "2019" @default.
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