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Dataset for dynamics and conformational changes in human NEIL2 protein analyzed by integrative structural biology approach Full article

Journal Data in Brief
ISSN: 2352-3409
Output data Year: 2022, Volume: 40, Article number : 107760, Pages count : DOI: 10.1016/j.dib.2021.107760
Tags Base excision repair; DNA damage; DNA glycosylases; DNA repair; HDX-MS; Molecular dynamics; NEIL2; Structural dynamics
Authors Zhdanova P.V. 1,2 , Ishchenko A.A. 3,4 , Chernonosov A.A. 1 , Zharkov D.O. 1,2 , Koval V.V. 1,2
Affiliations
1 Institute of Chemical Biology and Fundamental Medicine SB RAS, Novosibisk, Russian Federation
2 Novosibirsk State University, Novosibisk, Russian Federation
3 Groupe «Réparation de l'ADN», Equipe Labellisée par la Ligue Nationale contre le Cancer, CNRS UMR 8200, Univ. Paris-Sud, Université Paris-Saclay, Villejuif, F-94805, France
4 Gustave Roussy, Université Paris-Saclay, Villejuif, F-94805, France

Abstract: This work presents new data on human endonuclease VIII-like 2 protein (hNEIL2), a part of DNA glycosylases of the helix–two-turn–helix structural superfamily. While X-ray structure of oNEIL2 (opossum Monodelphis) was resolved partially [1], the structure of hNEIL2 has not yet been determined. This data article describes a powerful combination of hydrogen-deuterium exchange mass spectrometry, homology modeling, and molecular dynamics simulations for protein conformational dynamics analysis. The data supplied in this work are related to the research article entitled “Dynamics and Conformational Changes in Human NEIL2 DNA Glycosylase Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry”. © 2021
Cite: Zhdanova P.V. , Ishchenko A.A. , Chernonosov A.A. , Zharkov D.O. , Koval V.V.
Dataset for dynamics and conformational changes in human NEIL2 protein analyzed by integrative structural biology approach
Data in Brief. 2022. V.40. 107760 . DOI: 10.1016/j.dib.2021.107760 WOS Scopus РИНЦ OpenAlex
Dates:
Published online: Jan 30, 2022
Identifiers:
Web of science: WOS:000780046700016
Scopus: 2-s2.0-85121788925
Elibrary: 47550702
OpenAlex: W4200459250
Citing:
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Scopus 1
Elibrary 1
OpenAlex 2
Web of science 1
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