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  1. H-2. ナノ生命科学研究所
  2. h-2 10.学術雑誌掲載論文
  3. 1. 査読済論文

High-speed AFM reveals accelerated binding of agitoxin-2 to a K+ channel by induced fit

https://doi.org/10.24517/00054798
https://doi.org/10.24517/00054798
7156656d-135f-4eb0-bfee-563179d3a15d
名前 / ファイル ライセンス アクション
FR-PR-SUMIKAMA-T-0495.pdf FR-PR-SUMIKAMA-T-0495.pdf (988.6 kB)
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Item type 学術雑誌論文 / Journal Article(1)
公開日 2019-07-05
タイトル
タイトル High-speed AFM reveals accelerated binding of agitoxin-2 to a K+ channel by induced fit
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
ID登録
ID登録 10.24517/00054798
ID登録タイプ JaLC
著者 Sumino, Ayumi

× Sumino, Ayumi

WEKO 86313
e-Rad 80717140

Sumino, Ayumi

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Sumikama, Takashi

× Sumikama, Takashi

WEKO 84157
e-Rad 30579412

Sumikama, Takashi

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Uchihashi, T.

× Uchihashi, T.

WEKO 86315

Uchihashi, T.

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Oki, S.

× Oki, S.

WEKO 86316

Oki, S.

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著者別表示 角野, 歩

× 角野, 歩

角野, 歩

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炭竈, 享司

× 炭竈, 享司

炭竈, 享司

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提供者所属
内容記述タイプ Other
内容記述 金沢大学ナノ生命科学研究所
書誌情報 Science Advances

巻 5, 号 7, p. eaax0495, 発行日 2019-07-03
ISSN
収録物識別子タイプ ISSN
収録物識別子 2375-2548
DOI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 10.1126/sciadv.aax0495
出版者
出版者 American Association for the Advancement of Science
抄録
内容記述タイプ Abstract
内容記述 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.
権利
権利情報 Copyright © 2019The Authors, somerights reserved;exclusive licenseeAmerican Associationfor the Advancementof Science. No claim tooriginal U.S. GovernmentWorks. Distributedunder a CreativeCommons AttributionNonCommercialLicense 4.0 (CC BY-NC).
著者版フラグ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連URI
識別子タイプ URI
関連識別子 https://advances.sciencemag.org/content/5/7/eaax0495
関連名称 https://advances.sciencemag.org/content/5/7/eaax0495
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