Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding

Research output: Contribution to journalArticle

8 Citations (Scopus)

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 languageEnglish
Pages (from-to)680-686
Number of pages7
JournalFEBS Letters
Volume589
Issue number6
DOIs
Publication statusPublished - Mar 12 2015

Fingerprint

Purinergic P2X4 Receptors
Rats
Metals
Head
Cations
Adenosine Triphosphate
Nuclear magnetic resonance
Purinergic P2 Receptors
Crystallography
Zebrafish
Cell membranes
Disulfides
Metal ions
Binding Sites
Cell Membrane
Ions

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

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 journalArticle

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