Abstract
Background: The 5-hydroxytryptamine receptor (5-HT3R) is a prototypical pentameric ligand-gated ion channel. Results: The receptor's thermal stability was investigated in native plasma membranes, in detergent solution, and in reconstituted lipid bilayers. Conclusion: Unfolding of the 5-HT3R occurs via hierarchical, consecutive structural transitions, which can be distinguished experimentally. Significance: Our findings serve as an important base to create receptors of increased stability for structural/functional studies. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
| Original language | English |
|---|---|
| Pages (from-to) | 5756-5769 |
| Number of pages | 14 |
| Journal | The Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 22-Feb-2013 |
| Externally published | Yes |
Keywords
- ion channel
- serotonin 3 receptor
- serotonin receptor
- animal cell
- article
- beta sheet
- binding affinity
- cell membrane
- controlled study
- ligand binding
- lipid bilayer
- mouse
- nonhuman
- priority journal
- protein aggregation
- protein function
- protein localization
- protein refolding
- protein secondary structure
- protein unfolding
- temperature dependence
- thermostability