The crystal structure of a natural DNA polymerase complexed with mirror DNA

Authors
An, JinsuChoi, JaewooHwang, DohyeonPark, JihyunPemble, Charles W.Thi Hoai Men DuongKim, Kyoung-RanAhn, HeechulChung, Hak SukAhn, Dae-Ro
Issue Date
2020-02
Publisher
ROYAL SOC CHEMISTRY
Citation
CHEMICAL COMMUNICATIONS, v.56, no.14, pp.2186 - 2189
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.
Keywords
DELIVERY; NANOSTRUCTURES; REPLICATION; SPIEGELMER; MECHANISM; FIDELITY; SYSTEM; DNA polymerase; L-DNA duplex; protein crystallography; unnatural nucleic acid
ISSN
1359-7345
URI
https://pubs.kist.re.kr/handle/201004/119003
DOI
10.1039/c9cc09351f
Appears in Collections:
KIST Article > 2020
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE