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Description
金沢大学ナノ生命科学研究所
Agitoxin-2 (AgTx2) from scorpion venom is a potent blocker of K+ channels. The docking model has been elucidated, but it remains unclear whether binding dynamics are described by a two-state model (AgTx2-bound and AgTx2-unbound) or a more complicated mechanism, such as induced fit or conformational selection. Here, we observed the binding dynamics of AgTx2 to the KcsA channel using high-speed atomic force microscopy. From images of repeated binding and dissociation of AgTx2 to the channel, single-molecule kinetic analyses revealed that the affinity of the channel for AgTx2 increased during persistent binding and decreased during persistent dissociation. We propose a four-state model, including high- and low-affinity states of the channel, with relevant rate constants. An induced-fit pathway was dominant and accelerated binding by 400 times. This is the first analytical imaging of scorpion toxin binding in real time, which is applicable to various biological dynamics including channel ligands, DNA-modifier proteins, and antigen-antibody complexes.
Journal
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- Science Advances
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Science Advances 5 (7), eaax0495-, 2019-07-03
American Association for the Advancement of Science
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Details 詳細情報について
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- CRID
- 1390290700175914624
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- NII Article ID
- 120006649788
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- ISSN
- 23752548
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- Web Site
- http://hdl.handle.net/2297/00054798
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- JaLC
- IRDB
- CiNii Articles