Ontology highlight
ABSTRACT:
SUBMITTER: Hausmann R
PROVIDER: S-EPMC3340182 | biostudies-literature | 2012 Apr
REPOSITORIES: biostudies-literature
Hausmann Ralf R Bodnar Mandy M Woltersdorf Ronja R Wang Haihong H Fuchs Martin M Messemer Nanette N Qin Ying Y Günther Janka J Riedel Thomas T Grohmann Marcus M Nieber Karen K Schmalzing Günther G Rubini Patrizia P Illes Peter P
The Journal of biological chemistry 20120229 17
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 mutants in HEK293 cells to yield the P2X2 WT/P2X3 mutant or P2X2 mutant/P2X3 WT receptor ...[more]