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The prevalence of aromatic residues in the ligand binding site of the GABAA receptor, as with other cys‐loop ligand‐gated ion channels, is undoubtedly important for the ability of neurotransmitters to bind and trigger channel opening. Here, we have examined three conserved tyrosine residues at the GABA binding pocket (β2Tyr97, β2Tyr157, and β2Tyr205), making mutations to alanine and phenylalanine...
J. Neurochem. (2011) 119, 283–293.
AbstractThe GABAA receptor is an oligopentameric chloride channel that is activated via conformation changes induced upon the binding of the endogenous ligand, GABA, to the extracellular inter‐subunit interfaces. Although dozens of amino acid residues at the α/β interface have been implicated in ligand binding, the structural elements that mediate ligand binding...
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