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X-ray structures of AMPA receptor–cone snail toxin complexes illuminate activation mechanism
Author(s) -
Lei Chen,
Katharina L. Dürr,
Eric Gouaux
Publication year - 2014
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.1258409
Subject(s) - ampa receptor , snail , mechanism (biology) , toxin , biophysics , chemistry , receptor , microbiology and biotechnology , biology , physics , biochemistry , glutamate receptor , ecology , quantum mechanics
Activating a receptor to excite a neuron Transmitting signals between nerve cells, occuring at structures known as synapses, is critical to processes such as learning and memory. Fast transmission occurs when glutamate is released from a presynaptic neuron and binds to ionotropic glutamate receptors (iGluRs) in the cell membrane of a postsynaptic neuron. The iGluR contains an ion channel that is transiently opened, to activate the postsynaptic neuron, but then closes rapidly. Chenet al. and Yelshanskayaet al. report crystal structures in a range of conformations that together provide insight into how glutamate binding causes the channel to open and how other molecules that bind to the receptor modulate this. The information could aid in the design of drugs to treat cognitive impairment or seizure disordersScience , this issue p.1021 and p.1070

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