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P2X receptor channels show three-fold symmetry in ionic charge selectivity and unitary conductance
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 Thr(339). Replacing Thr(339) by lysine in one, two or three subunits progressively increased chloride permeability and reduced unitary cond...
Autores principales: | Browne, Liam E., Cao, Lishuang, Broomhead, Helen E., Bragg, Laricia, Wilkinson, William, North, R. Alan |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3012030/ https://www.ncbi.nlm.nih.gov/pubmed/21170052 http://dx.doi.org/10.1038/nn.2705 |
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