Extracellular proton alters the divalent cation binding affinity in a cyclic nucleotide-gated channel pore.

doi:10.1016/s0014-5793(98)01353-2

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Article

Extracellular proton alters the divalent cation binding affinity in a cyclic nucleotide-gated channel pore.

FEBS letters - 27 Nov 1998

Rho S H, Park C S

Abstract excerpt

Extracellular protons in the range of 10(-9) to 10(-5) M effectively suppressed Na+ current (K(1/2) = 10(-6.1)) through the bovine retinal guanosine 3',5'-cyclic mononucleotide-gated ion channel expressed in Xenopus oocytes. The reduction of channel current was mediated by a single glutamate resi...

Topics

Amino Acid Substitution
Animals
Binding Sites
Cations, Divalent
Cattle
Cyclic Nucleotide-Gated Cation Channels
Electrophysiology
Glutamic Acid
Hydrogen-Ion Concentration
Ion Channels
Mutation
Oocytes
Protons
Sodium
Static Electricity
Strontium
Titrimetry
Xenopus laevis

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