TY - JOUR
T1 - Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding
AU - Igawa, Tatsuhiro
AU - Abe, Yoshito
AU - Tsuda, Makoto
AU - Inoue, Kazuhide
AU - Ueda, Tadashi
N1 - Funding Information:
We thank Dr. M. Shiroishi, Graduate School of Pharmaceutical Sciences, Kyushu University, for valuable comments, Dr. N. Ito and Dr. T. Ikura, Research Institute for Biomedical Sciences, Tokyo University of Science, for helping us perform ITC experiments, and KN International and Edanz Group Ltd. for improving the English use in our manuscript. This work was supported by Japan Society for the Promotion of Science (JSPS) KAKENHI Grant Nos. 26293129 and 23390155 to YA and TU and by a Grant-in-Aid for JSPS Fellows to TI. The work for the ITC measurements was supported by the Platform for Drug Discovery, Informatics, and Structural Life Science from the Ministry of Education, Culture, Sports, Science, and Technology, Japan.
Publisher Copyright:
© 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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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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 -