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P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
Ist Teil von
Nature neuroscience, 2010-12, Vol.14 (1), p.17-18
Ort / Verlag
Nature Publishing Group
Erscheinungsjahr
2010
Quelle
EBSCOhost Psychology and Behavioral Sciences Collection
Beschreibungen/Notizen
In the closed structure of the P2X cation channel, three α-helical transmembrane domains cross the membrane obliquely: in rat P2X2 receptors, these intersect at Thr339. Replacing Thr339 by lysine in one, two or three subunits progressively increased chloride permeability and reduced unitary conductance. This implies that the closed-open transition involves a symmetrical separation of the three subunits, and that Thr339 from each contributes symmetrically to the open channel permeation pathway.