Structural titration of receptor ion channel GLIC gating by HS-AFM Journal Article
| Authors: | Ruan, Y.; Kao, K.; Lefebvre, S.; Marchesi, A.; Corringer, P. J.; Hite, R. K.; Scheuring, S. |
| Article Title: | Structural titration of receptor ion channel GLIC gating by HS-AFM |
| Abstract: | Gloeobacter violaceus ligand-gated ion channel (GLIC), a protongated, cation-selective channel, is a prokaryotic homolog of the pentameric Cys-loop receptor ligand-gated ion channel family. Despite large changes in ion conductance, small conformational changes were detected in X-ray structures of detergent-solubilized GLIC at pH 4 (active/desensitized state) and pH 7 (closed state). Here, we used high-speed atomic force microscopy (HS-AFM) combined with a buffer exchange system to performstructural titration experiments to visualize GLIC gating at the single-molecule level under native conditions. Reference-free 2D classification revealed channels in multiple conformational states during pH gating. We find changes of protein-protein interactions so far elusive and conformational dynamics much larger than previously assumed. Asymmetric pentamers populate early stages of activation, which provides evidence for an intermediate preactivated state. © 2018 National Academy of Sciences.All Rights Reserved. |
| Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
| Volume: | 115 |
| Issue: | 41 |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Date Published: | 2018-10-09 |
| Start Page: | 10333 |
| End Page: | 10338 |
| Language: | English |
| DOI: | 10.1073/pnas.1805621115 |
| PUBMED: | 30181288 |
| PROVIDER: | scopus |
| PMCID: | PMC6187180 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 1 November 2018 -- Source: Scopus |
Altmetric
Citation Impact
BMJ Impact Analytics
Related MSK Work