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Article

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

Structure (London, England : 1993) - 1 Nov 2003

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

Abstract excerpt

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...

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Identifiers

PMID: 14604528
DOI: 10.1016/j.str.2003.10.003

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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