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Structural Basis of the KcsA K+Channel and Agitoxin2 Pore-Blocking Toxin Interaction by Using the Transferred Cross-Saturation Method

Authors
Journal
Structure
0969-2126
Publisher
Elsevier
Publication Date
Volume
11
Issue
11
Identifiers
DOI: 10.1016/j.str.2003.10.003

Abstract

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.

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