Cysteine Scanning Mutagenesis (Residues Glu52–Gly96) of the Human P2X1 Receptor for ATP

@inproceedings{Allsopp2011CysteineSM,
  title={Cysteine Scanning Mutagenesis (Residues Glu52–Gly96) of the Human P2X1 Receptor for ATP},
  author={Rebecca C. Allsopp and Sam El Ajouz and Ralf S Schmid and Richard J. Evans},
  booktitle={The Journal of biological chemistry},
  year={2011}
}
P2X receptors are ATP-gated cation channels. The x-ray structure of a P2X4 receptor provided a major advance in understanding the molecular basis of receptor properties. However, how agonists are coordinated, the extent of the binding site, and the contribution of the vestibules in the extracellular domain to ionic permeation have not been addressed. We have used cysteine-scanning mutagenesis to determine the contribution of residues Glu(52)-Gly(96) to human P2X1 receptor properties. ATP… CONTINUE READING

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