Structural basis of the KcsA K+ channel and agitoxin2 pore-blocking toxin interaction by using the transferred cross-saturation method

Koh Takeuchi, Mariko Yokogawa, Tomoki Matsuda, Mariko Sugai, Seiko Kawano, Toshiyuki Kohno, Haruki Nakamura, Hideo Takahashi, Ichio Shimada

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)

Abstract

We have determined the binding site on agitoxin2 (AgTx2) to the KcsA K + channel by a transferred cross-saturation (TCS) experiment. The residues significantly affected in the TCS experiments formed a contiguous surface on AgTx2, and substitutions of the surface residues decreased the binding affinity to the KcsA K+ channel. Based on properties of the AgTx2 binding site with the KcsA K+ channel, we present a surface motif that is observed in pore-blocking toxins affecting the K+ channel. Furthermore, we also explain the structural basis of the specificity of the K+ channel to the toxins. The TCS method utilized here is applicable not only for the channels, which are complexed with other inhibitors, but also with a variety of regulatory molecules, and provides important information about their interface in solution.

Original languageEnglish
Pages (from-to)1381-1392
Number of pages12
JournalStructure
Volume11
Issue number11
DOIs
Publication statusPublished - 2003 Nov
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Structural basis of the KcsA K<sup>+</sup> channel and agitoxin2 pore-blocking toxin interaction by using the transferred cross-saturation method'. Together they form a unique fingerprint.

Cite this