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  1. H220 細胞生理学研究センター
  2. H220a 雑誌掲載論文
  3. 学術雑誌

Optimized expression and purification of NavAb provide the structural insight into the voltage dependence

http://hdl.handle.net/2237/00027957
http://hdl.handle.net/2237/00027957
9b9933eb-ad00-4547-9c4e-eff4fba842cc
名前 / ファイル ライセンス アクション
Revised_FEBSL-17-1362_R1_proof_kirie_docx.pdf Revised_FEBSL-17-1362_R1_proof_kirie_docx (3.0 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2018-05-10
タイトル
タイトル Optimized expression and purification of NavAb provide the structural insight into the voltage dependence
言語 en
著者 Irie, Katsumasa

× Irie, Katsumasa

WEKO 76401

en Irie, Katsumasa

Search repository
Haga, Yukari

× Haga, Yukari

WEKO 76402

en Haga, Yukari

Search repository
Shimomura, Takushi

× Shimomura, Takushi

WEKO 76403

en Shimomura, Takushi

Search repository
Fujiyoshi, Yoshinori

× Fujiyoshi, Yoshinori

WEKO 76404

en Fujiyoshi, Yoshinori

Search repository
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利
言語 en
権利情報 This is the peer reviewed version of the following article: [Irie, K. , Haga, Y. , Shimomura, T. and Fujiyoshi, Y. (2018), Optimized expression and purification of NavAb provide the structural insight into the voltage dependence. FEBS Lett, 592: 274-283. doi:10.1002/1873-3468.12955], which has been published in final form at [https://doi.org/10.1002/1873-3468.12955]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
キーワード
主題Scheme Other
主題 protein expression
キーワード
主題Scheme Other
主題 structural physiology
キーワード
主題Scheme Other
主題 voltage‐gated sodium channel
抄録
内容記述 Voltage‐gated sodium channels are crucial for electro‐signalling in living systems. Analysis of the molecular mechanism requires both fine electrophysiological evaluation and high‐resolution channel structures. Here, we optimized a dual expression system of NavAb, which is a well‐established standard of prokaryotic voltage‐gated sodium channels, for E. coli and insect cells using a single plasmid vector to analyse high‐resolution protein structures and measure large ionic currents. Using this expression system, we evaluated the voltage dependence and determined the crystal structures of NavAb wild‐type and two mutants, E32Q and N49K, whose voltage dependence were positively shifted and essential interactions were lost in voltage sensor domain. The structural and functional comparison elucidated the molecular mechanisms of the voltage dependence of prokaryotic voltage‐gated sodium channels.
言語 en
内容記述タイプ Abstract
内容記述
内容記述 ファイル公開:2019-01-09
言語 ja
内容記述タイプ Other
出版者
言語 en
出版者 Wiley
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1002/1873-3468.12955
ISSN
収録物識別子タイプ PISSN
収録物識別子 00145793
書誌情報 en : FEBS Letters

巻 592, 号 2, p. 274-283, 発行日 2018-01
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