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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/80524499c4df7-05e9-4d40-a464-ee95df6fc0fe
Item type | 会議発表用資料 / Presentation(1) | |||||
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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× Hirano, Yuu× Tamada, Taro× Kono, Hidetoshi× Sunami, Tomoko× Hirano, Yuu× Tamada, Taro× Kono, Hidetoshi |
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抄録 | ||||||
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 |