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

id	doaj-2dff6c27b8244f03bdfbb18f51738a7b
record_format	Article
spelling	doaj-2dff6c27b8244f03bdfbb18f51738a7b2021-05-11T10:01:47ZengNature Publishing GroupNature Communications2041-17232018-01-019111310.1038/s41467-017-02530-zStructural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1Fiona J. Flett0Emilija Ruksenaite1Lee A. Armstrong2Shipra Bharati3Roberta Carloni4Elizabeth R. Morris5C. Logan Mackay6Heidrun Interthal7Julia M. Richardson8Institute of Cell Biology, School of Biological Sciences, University of EdinburghInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, University of EdinburghInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, University of EdinburghInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, University of EdinburghInstitute of Cell Biology, School of Biological Sciences, University of EdinburghInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, University of EdinburghEaStCHEM School of Chemistry, University of EdinburghInstitute of Cell Biology, School of Biological Sciences, University of EdinburghInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, University of EdinburghHuman 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.https://doi.org/10.1038/s41467-017-02530-z
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Fiona J. Flett Emilija Ruksenaite Lee A. Armstrong Shipra Bharati Roberta Carloni Elizabeth R. Morris C. Logan Mackay Heidrun Interthal Julia M. Richardson
spellingShingle	Fiona J. Flett Emilija Ruksenaite Lee A. Armstrong Shipra Bharati Roberta Carloni Elizabeth R. Morris C. Logan Mackay Heidrun Interthal Julia M. Richardson Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1 Nature Communications
author_facet	Fiona J. Flett Emilija Ruksenaite Lee A. Armstrong Shipra Bharati Roberta Carloni Elizabeth R. Morris C. Logan Mackay Heidrun Interthal Julia M. Richardson
author_sort	Fiona J. Flett
title	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_short	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_full	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_fullStr	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_full_unstemmed	Structural basis for DNA 3′-end processing by human tyrosyl-DNA phosphodiesterase 1
title_sort	structural basis for dna 3′-end processing by human tyrosyl-dna phosphodiesterase 1
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-01-01
description	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.
url	https://doi.org/10.1038/s41467-017-02530-z
work_keys_str_mv	AT fionajflett structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1 AT emilijaruksenaite structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1 AT leeaarmstrong structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1 AT shiprabharati structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1 AT robertacarloni structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1 AT elizabethrmorris structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1 AT cloganmackay structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1 AT heidruninterthal structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1 AT juliamrichardson structuralbasisfordna3endprocessingbyhumantyrosyldnaphosphodiesterase1
_version_	1721448809950609408

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

Similar Items