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Structural basis for an array of engrailed homeodomains toward the development of genome-editing enzymes

https://repo.qst.go.jp/records/80524
https://repo.qst.go.jp/records/80524
499c4df7-05e9-4d40-a464-ee95df6fc0fe
Item type 会議発表用資料 / Presentation(1)
公開日 2020-06-25
タイトル
タイトル Structural basis for an array of engrailed homeodomains toward the development of genome-editing enzymes
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_c94f
資源タイプ conference object
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Sunami, Tomoko

× Sunami, Tomoko

WEKO 891424

Sunami, Tomoko

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Hirano, Yuu

× Hirano, Yuu

WEKO 891425

Hirano, Yuu

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Tamada, Taro

× Tamada, Taro

WEKO 891426

Tamada, Taro

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Kono, Hidetoshi

× Kono, Hidetoshi

WEKO 891427

Kono, Hidetoshi

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Sunami, Tomoko

× Sunami, Tomoko

WEKO 891428

en Sunami, Tomoko

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Hirano, Yuu

× Hirano, Yuu

WEKO 891429

en Hirano, Yuu

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Tamada, Taro

× Tamada, Taro

WEKO 891430

en Tamada, Taro

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Kono, Hidetoshi

× Kono, Hidetoshi

WEKO 891431

en Kono, Hidetoshi

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内容記述タイプ Abstract
内容記述 A small DNA binding protein to target desired sequences have the potential to become a scaffold of molecular tools such as genome-editing enzymes. We previously showed two engrailed homeodomains (EHDs) connected with a linker recognizes a target sequence twice as long as a single EHD in cells only when arginine 53 in each EHD in the tandem protein is mutated to alanine ((EHD[R53A])2). In this study, we determined the crystal structure of the (EHD[R53A])2-DNA complex. Most importantly, it shows the base-specific interactions necessary for the affinity and/or specificity of the wild-type EHD are preserved in (EHD[R53A])2. The mechanism of the specific recognition will be discussed based on the structure and cellular assays.
会議概要(会議名, 開催地, 会期, 主催者等)
内容記述タイプ Other
内容記述 第58回日本生物物理学会年会
発表年月日
日付 2020-09-17
日付タイプ Issued
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