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 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding. / Igawa, Tatsuhiro; Abe, Yoshito; Makoto, Tsuda; Inoue, Kazuhide; Ueda, Tadashi.
In: FEBS Letters, Vol. 589, No. 6, 12.03.2015, p. 680-686.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding
AU - Igawa, Tatsuhiro
AU - Abe, Yoshito
AU - Makoto, Tsuda
AU - Inoue, Kazuhide
AU - Ueda, Tadashi
PY - 2015/3/12
Y1 - 2015/3/12
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=84923555624&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2015.01.034
DO - 10.1016/j.febslet.2015.01.034
M3 - Article
C2 - 25662851
AN - SCOPUS:84923555624
VL - 589
SP - 680
EP - 686
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 6
ER -