@misc{oai:repo.qst.go.jp:00080524,
 author = {Sunami, Tomoko and Hirano, Yuu and Tamada, Taro and Kono, Hidetoshi and Sunami, Tomoko and Hirano, Yuu and Tamada, Taro and Kono, Hidetoshi},
 month = {Sep},
 note = {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., 第58回日本生物物理学会年会},
 title = {Structural basis for an array of engrailed homeodomains toward the development of genome-editing enzymes},
 year = {2020}
}