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Article

Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals.

Proceedings of the National Academy of Sciences of the United States of America - 17 Apr 2012

Gonzalez-Gutierrez Giovanni, Lukk Tiit, Agarwal Vinayak, Papke David, Nair Satish K, Grosman Claudio

Abstract excerpt

The determination of structural models of the various stable states of an ion channel is a key step toward the characterization of its conformational dynamics. In the case of nicotinic-type receptors, different structures have been solved but, thus far, these different models have been obtained from different members of the superfamily. In the case of the bacterial member ELIC, a cysteamine-gated channel from...

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Identifiers

PMID: 22474383
DOI: 10.1073/pnas.1119268109
PMCID: PMC3341056

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Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals.PMID 22474383Read ↗

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