Extracellular proton alters the divalent cation binding affinity in a cyclic nucleotide-gated channel pore
نویسندگان
چکیده
منابع مشابه
Isolation of a Single Carboxyl-Carboxylate Proton Binding Site in the Pore of a Cyclic Nucleotide–Gated Channel
The pore of the catfish olfactory cyclic nucleotide-gated (CNG) channel contains four conserved glutamate residues, one from each subunit, that form a high-affinity binding site for extracellular divalent cations. Previous work showed that these residues form two independent and equivalent high-pKa (approximately 7.6) proton binding sites, giving rise to three pH-dependent conductance states, a...
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In classical tetrameric voltage-gated ion channels four voltage-sensing domains (VSDs), one from each subunit, control one ion permeation pathway formed by four pore domains. The human Hv1 proton channel has a different architecture, containing a VSD, but lacking a pore domain. Since its location is not known, we searched for the Hv permeation pathway. We find that mutation of the S4 segment's ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1998
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(98)01353-2