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Cited by 872

The DOI matches its Crossref record; 83 of the 83 references it cites were found in a registry or an index.

Mechanisms for Activation and Antagonism of an AMPA-Sensitive Glutamate Receptor

Open access
Armstrong, Neali, Gouaux, Eric·2000·Neuron

Abstract

Crystal structures of the GluR2 ligand binding core (S1S2) have been determined in the apo state and in the presence of the antagonist DNQX, the partial agonist kainate, and the full agonists AMPA and glutamate. The domains of the S1S2 ligand binding core are expanded in the apo state and contract upon ligand binding with the extent of domain separation decreasing in the order of apo > DNQX > kainate > glutamate approximately equal to AMPA. These results suggest that agonist-induced domain closure gates the transmembrane channel and the extent of receptor activation depends upon the degree of domain closure. AMPA and glutamate also promote a 180 degrees flip of a trans peptide bond in the ligand binding site. The crystal packing of the ligand binding cores suggests modes for subunit-subunit contact in the intact receptor and mechanisms by which allosteric effectors modulate receptor activity.

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Metadata

Authors
Armstrong, N., & Gouaux, E.
Venue
Neuron
Publisher
Elsevier BV
Published
2000-10
Volume
28
Issue
1
Pages
165-181
ISSN
0896-6273 (ISSN-L)
OpenAlex
W1922786159
Cited by
872
References
83
FWCI
15.70
Type
journal article
Language
en
Open access
hybrid

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Armstrong, N., & Gouaux, E. (2000). Mechanisms for Activation and Antagonism of an AMPA-Sensitive Glutamate Receptor. Neuron. https://doi.org/10.1016/s0896-6273(00)00094-5

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