Conformational transitions and allosteric modulation in a heteromeric glycine receptor

Eric Gibbs; Emily Klemm; David Seiferth; Arvind Kumar; Serban L. Ilca; Philip C. Biggin; Sudha Chakrapani

doi:10.1038/s41467-023-37106-7

Nature Communications (Mar 2023)

Conformational transitions and allosteric modulation in a heteromeric glycine receptor

Eric Gibbs,
Emily Klemm,
David Seiferth,
Arvind Kumar,
Serban L. Ilca,
Philip C. Biggin,
Sudha Chakrapani

Affiliations

Eric Gibbs: Department of Physiology and Biophysics, Case Western Reserve University
Emily Klemm: Department of Physiology and Biophysics, Case Western Reserve University
David Seiferth: Department of Biochemistry, University of Oxford
Arvind Kumar: Department of Physiology and Biophysics, Case Western Reserve University
Serban L. Ilca: New York Structural Biology Center
Philip C. Biggin: Department of Biochemistry, University of Oxford
Sudha Chakrapani: Department of Physiology and Biophysics, Case Western Reserve University

DOI: https://doi.org/10.1038/s41467-023-37106-7
Journal volume & issue: Vol. 14, no. 1
pp. 1 – 15

Abstract

Read online

Glycine receptors (GlyR) are a critical postsynaptic component of spinal neurons. Here, the auhtors present cryo-EM structures of a heteromeric GlyR in the presence of an antagonist, agonist and agonist with a positive allosteric modulator.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal