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Science 23 September 1994: Vol. 265. no. 5180, pp. 1852 - 1856 DOI: 10.1126/science.7522344
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Articles
Science, Vol 265, Issue 5180, 1852-1856
Copyright © 1994 by American Association for the Advancement of Science
Two identical noninteracting sites in an ion channel revealed by proton transfer
MJ Root
and
R MacKinnon
Department of Neurobiology, Harvard Medical School, Boston, MA 02115.
The functional consequences of single proton transfers occurring in the pore of a cyclic nucleotide-gated channel were observed with patch recording techniques. These results led to three conclusions about the chemical nature of ion binding sites in the conduction pathway: The channel contains two identical titratable sites, even though there are more than two (probably four) identical subunits; the sites are formed by glutamate residues that have a pKa (where K(a) is the acid constant) of 7.6; and protonation of one site does not perturb the pKa of the other. These properties point to an unusual arrangement of carboxyl side-chain residues in the pore of a cation channel.
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