Conformational transitions and allosteric modulation in a heteromeric glycine receptor
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.
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-37106-7 |
| _version_ | 1797864248487968768 |
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| author | Eric Gibbs Emily Klemm David Seiferth Arvind Kumar Serban L. Ilca Philip C. Biggin Sudha Chakrapani |
| author_facet | Eric Gibbs Emily Klemm David Seiferth Arvind Kumar Serban L. Ilca Philip C. Biggin Sudha Chakrapani |
| author_sort | Eric Gibbs |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-09T22:48:43Z |
| format | Article |
| id | doaj.art-db781d0d4fdb4137a11e404a9029e982 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-09T22:48:43Z |
| publishDate | 2023-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-db781d0d4fdb4137a11e404a9029e9822023-03-22T11:43:25ZengNature PortfolioNature Communications2041-17232023-03-0114111510.1038/s41467-023-37106-7Conformational transitions and allosteric modulation in a heteromeric glycine receptorEric Gibbs0Emily Klemm1David Seiferth2Arvind Kumar3Serban L. Ilca4Philip C. Biggin5Sudha Chakrapani6Department of Physiology and Biophysics, Case Western Reserve UniversityDepartment of Physiology and Biophysics, Case Western Reserve UniversityDepartment of Biochemistry, University of OxfordDepartment of Physiology and Biophysics, Case Western Reserve UniversityNew York Structural Biology CenterDepartment of Biochemistry, University of OxfordDepartment of Physiology and Biophysics, Case Western Reserve UniversityGlycine 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.https://doi.org/10.1038/s41467-023-37106-7 |
| spellingShingle | Eric Gibbs Emily Klemm David Seiferth Arvind Kumar Serban L. Ilca Philip C. Biggin Sudha Chakrapani Conformational transitions and allosteric modulation in a heteromeric glycine receptor Nature Communications |
| title | Conformational transitions and allosteric modulation in a heteromeric glycine receptor |
| title_full | Conformational transitions and allosteric modulation in a heteromeric glycine receptor |
| title_fullStr | Conformational transitions and allosteric modulation in a heteromeric glycine receptor |
| title_full_unstemmed | Conformational transitions and allosteric modulation in a heteromeric glycine receptor |
| title_short | Conformational transitions and allosteric modulation in a heteromeric glycine receptor |
| title_sort | conformational transitions and allosteric modulation in a heteromeric glycine receptor |
| url | https://doi.org/10.1038/s41467-023-37106-7 |
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