Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1

Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1

Human tyrosyl-DNA phosphodiesterase 1 (Tdp1) repairs covalently trapped topoisomerase 1B-DNA complexes and other lesions, and is a target for anticancer drug development. Here the authors use an integrated structural approach to shed light onto the molecular basis of DNA end-processing by Tdp1.

Bibliographic Details
Main Authors: Fiona J. Flett, Emilija Ruksenaite, Lee A. Armstrong, Shipra Bharati, Roberta Carloni, Elizabeth R. Morris, C. Logan Mackay, Heidrun Interthal, Julia M. Richardson
Format: Article
Language:English
Published: Nature Publishing Group 2018-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02530-z
Description
Summary:Human tyrosyl-DNA phosphodiesterase 1 (Tdp1) repairs covalently trapped topoisomerase 1B-DNA complexes and other lesions, and is a target for anticancer drug development. Here the authors use an integrated structural approach to shed light onto the molecular basis of DNA end-processing by Tdp1.
ISSN:2041-1723

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