title: Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding.
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.
authors: Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.
authors: Tatsuhiro
authors: T
authors: Igawa
authors: Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.
authors: Yoshito
authors: Y
authors: Abe
authors: Department of Molecular and System Pharmacology, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.
authors: Makoto
authors: M
authors: Tsuda
authors: Department of Molecular and System Pharmacology, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.
authors: Kazuhide
authors: K
authors: Inoue
authors: Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan. Electronic address: ueda@phar.kyushu-u.ac.jp.
authors: Tadashi
authors: T
authors: Ueda
mesh_terms: D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000737:chemistry; D003553:Cystine / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D051381:Rats; D058848:Receptors, Purinergic P2X4 / Q000737:chemistry*; D012996:Solutions; D015032:Zinc / Q000737:chemistry
chemical_list: D058848:Receptors, Purinergic P2X4; D012996:Solutions; D003553:Cystine; D003300:Copper; D015032:Zinc
keywords: Head domain; Metal binding; NMR; P2X4 receptor; Protein structure