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Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel.

Abstract：

:Charybdotoxin (CTX) blocks high conductance Ca(2+)-activated K+ channels by binding to a receptor site in the externally facing "mouth." Toxin bound to the channel can be destabilized from its site by K+ entering the channel from the opposite, internal, solution. By analyzing point mutants of CTX expressed in E. coli, assayed with single Ca(2+)-activated K+ channels reconstituted into planar lipid bilayers, we show that a single positively charged residue of the peptide, Lys-27, wholly mediates this interaction of K+ with CTX. If position 27 carries a positively charged residue, internal K+ accelerates the dissociation rate of CTX in a voltage-dependent manner; however, if a neutral Asn or Gln is substituted at this position, the dissociation rate is completely insensitive to either internal K+ or applied voltage. Position 27 is unique in this respect; charge-neutral substitutions made at other positions fail to eliminate the K+ destabilization phenomenon. The results argue that CTX bound to the channel positions Lys-27 physically close to a K(+)-specific binding site on the external end of the conduction pathway and that a K+ ion occupying this site destabilizes CTX via direct electrostatic repulsion with the epsilon-amino group of Lys-27.

journal_name

Neuron

journal_title

Neuron

authors

Park CS,Miller C

doi

10.1016/0896-6273(92)90169-e

subject

Has Abstract

pub_date

1992-08-01 00:00:00

pages

307-13

issue

2

eissn

0896-6273

issn

1097-4199

pii

0896-6273(92)90169-E

journal_volume

9

pub_type

杂志文章

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