Article
Differential role of extracellular histidines in copper, zinc, magnesium and proton modulation of the P2X7 purinergic receptor.
Journal of neurochemistry - 1 Apr 2007
Acuña-Castillo Claudio, Coddou Claudio, Bull Paulina, Brito Jocelyn, Huidobro-Toro J Pablo
Abstract excerpt
The P2X7 receptor is a non-selective cationic channel activated by extracellular ATP, belonging to the P2X receptor family. To assess the role of extracellular histidines on the allosteric modulation of the rat P2X7 receptor by divalent metals (copper, zinc and magnesium) and protons, these amino acid residues were singly substituted for corresponding alanines. Wild-type and mutated receptors were injected to...
Topics
- Adenosine Triphosphate
- Allosteric Regulation
- Animals
- Binding Sites
- Cations, Divalent
- Cell Membrane
- Copper
- Extracellular Fluid
- Female
- Histidine
- Hydrogen-Ion Concentration
- Ion Channel Gating
- Magnesium
- Metals