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Article

ATP binding site mutagenesis reveals different subunit stoichiometry of functional P2X2/3 and P2X2/6 receptors.

The Journal of biological chemistry - 20 Apr 2012

Hausmann Ralf, Bodnar Mandy, Woltersdorf Ronja, Wang Haihong, Fuchs Martin, Messemer Nanette, Qin Ying, Günther Janka, Riedel Thomas, Grohmann Marcus, Nieber Karen, Schmalzing Günther, Rubini Patrizia, Illes Peter

Abstract excerpt

The aim of the present experiments was to clarify the subunit stoichiometry of P2X2/3 and P2X2/6 receptors, where the same subunit (P2X2) forms a receptor with two different partners (P2X3 or P2X6). For this purpose, four non-functional Ala mutants of the P2X2, P2X3, and P2X6 subunits were generated by replacing single, homologous amino acids particularly important for agonist binding. Co-expression of these...

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PMID: 22378790
DOI: 10.1074/jbc.M112.345207
PMCID: PMC3340182

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