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Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1721349205

Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

About this item

Full title

Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2015-10, Vol.526 (7572), p.277-280

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The X-ray crystal structure of the human glycine receptor in the presence of strychnine, an antagonist, reveals how antagonist binding leads to closure of the channel pore.
Structure of human GlyR
The strychnine-sensitive glycine receptor (GlyR) mediates neurotransmission throughout the spinal cord and brainstem. These ligand-gated channels c...

Alternative Titles

Full title

Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_1721349205

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1721349205

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature14972

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