한빛사 논문
Jinsu An‡,a,b, Jaewoo Choi‡,a, Dohyeon Hwang‡,a, Jihyun Parka, Charles W. Pemble, IVc, Thi Hoai Men Duongd, Kyoung-Ran Kima, Heechul Ahnd, Hak Suk Chung*,a,b and Dae-Ro Ahn*,a,b
aCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology (KIST), Hwarangno 14-gil 5, Seongbuk-gu, Seoul 02792, Republic of Korea
bDivision of Bio-Medical Science and Technology, KIST School, University of Science and Technology (UST), Seoul 02792, Republic of Korea
cRigaku Americas Corporation, 9009 New Trails Drive, The Woodlands, TX, USA
dDepartment of Pharmacy, Dongguk University-Seoul, 32 Dongguk-ro, Ilsandong-gu, Goyang, Gyeonggi 13024, Republic of Korea
*Corresponding authors
‡ These authors contributed equally.
Abstract
The intrinsic L-DNA binding properties of a natural DNA polymerase was discovered. The binding affinity of Dpo4 polymerase for L-DNA was comparable to that for D-DNA. The crystal structure of Dpo4/L-DNA complex revealed a dimer formed by the little finger domain that provides a binding site for L-DNA.
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