PUBLICATION
Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding
- Authors
- Igawa, T., Abe, Y., Tsuda, M., Inoue, K., Ueda, T.
- ID
- ZDB-PUB-150211-23
- Date
- 2015
- Source
- FEBS letters 589(6): 680-6 (Journal)
- Registered Authors
- Keywords
- Head domain, Metal binding, NMR, P2X4 receptor, Protein structure
- MeSH Terms
-
- Protein Structure, Tertiary
- Animals
- Zinc/chemistry
- Rats
- Nuclear Magnetic Resonance, Biomolecular
- Solutions
- Models, Molecular
- Protein Binding
- Receptors, Purinergic P2X4/chemistry*
- Copper/chemistry
- Cystine/chemistry
- Binding Sites
- PubMed
- 25662851 Full text @ FEBS Lett.
Citation
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):680-6.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping