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Article

Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels.

Scientific reports - 12 Sept 2016

Fryatt Alistair G, Dayl Sudad, Cullis Paul M, Schmid Ralf, Evans Richard J

Abstract excerpt

Structural studies of P2X receptors show a novel U shaped ATP orientation following binding. We used voltage clamp fluorometry (VCF) and molecular dynamics (MD) simulations to investigate agonist action. For VCF the P2X1 receptor (P2X1R) K190C mutant (adjacent to the agonist binding pocket) was labelled with the fluorophore MTS-TAMRA and changes in fluorescence on agonist treatment provided a real time measure of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 27616669
DOI: 10.1038/srep32918
PMCID: PMC5018734

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