Abstract
The P2X receptor is an ATP-gated cation channel expressed on the plasma membrane. The head domain (Gln111-Val167 in the rat P2X4 receptor) regulates ATP-induced cation influx. In this study, we prepared a head domain with three disulfide bonds, such as the intact rat P2X4 receptor contains. NMR analysis showed that the head domain possessed the same fold as in the zebrafish P2X4 receptor previously determined by crystallography. Furthermore, the inhibitory, divalent, metal ion binding sites were determined by NMR techniques. These findings will be useful for the design of specific inhibitors for the P2X receptor family.
| Original language | English |
|---|---|
| Pages (from-to) | 680-686 |
| Number of pages | 7 |
| Journal | FEBS Letters |
| Volume | 589 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Mar 12 2015 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Igawa, T., Abe, Y., Tsuda, M., Inoue, K., & Ueda, T. (2015). Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding. FEBS Letters, 589(6), 680-686. https://doi.org/10.1016/j.febslet.2015.01.034