X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors

Thorsten Althoff, Ryan E. Hibbs, Surajit Banerjee and Eric Gouaux ()
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Thorsten Althoff: Vollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA
Ryan E. Hibbs: Vollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA
Surajit Banerjee: NE-CAT/Cornell University, 9700 South Cass Avenue, Building 436 E001, Argonne, Illinois 60439, USA
Eric Gouaux: Vollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, USA

Nature, 2014, vol. 512, issue 7514, 333-337

Abstract: This study solved structures of the glutamate-gated chloride channel (GluCl), a Cys-loop receptor from C. elegans, in an apo, closed state and in a lipid-bound state — comparison of these structures with a previously published structure of GluCl in an ivermectin-bound state reveals what conformational changes probably occur as this membrane protein transitions from the closed/resting state towards an open/activated state.

Date: 2014
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DOI: 10.1038/nature13669

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