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Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA

The purpose of the present review is to summarize the data related with the structural features of interaction between the human repair enzyme 8-oxoguanine DNA glycosylase (hOGG1) and DNA. The review covers the questions concerning the role of individual amino acids of hOGG1 in the specific recognit...

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Autores principales: Koval, V. V., Knorre, D. G., Fedorova, O. S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4207560/
https://www.ncbi.nlm.nih.gov/pubmed/25349714
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author Koval, V. V.
Knorre, D. G.
Fedorova, O. S.
author_facet Koval, V. V.
Knorre, D. G.
Fedorova, O. S.
author_sort Koval, V. V.
collection PubMed
description The purpose of the present review is to summarize the data related with the structural features of interaction between the human repair enzyme 8-oxoguanine DNA glycosylase (hOGG1) and DNA. The review covers the questions concerning the role of individual amino acids of hOGG1 in the specific recognition of the oxidized DNA bases, formation of the enzyme–substrate complex, and excision of the lesion bases from DNA. Attention is also focused upon conformational changes in the enzyme active site and disruption of enzyme activity as a result of amino acid mutations. The mechanism of damaged bases release from DNA induced by hOGG1 is discussed in the context of structural dynamics.
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spelling pubmed-42075602014-10-27 Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA Koval, V. V. Knorre, D. G. Fedorova, O. S. Acta Naturae Research Article The purpose of the present review is to summarize the data related with the structural features of interaction between the human repair enzyme 8-oxoguanine DNA glycosylase (hOGG1) and DNA. The review covers the questions concerning the role of individual amino acids of hOGG1 in the specific recognition of the oxidized DNA bases, formation of the enzyme–substrate complex, and excision of the lesion bases from DNA. Attention is also focused upon conformational changes in the enzyme active site and disruption of enzyme activity as a result of amino acid mutations. The mechanism of damaged bases release from DNA induced by hOGG1 is discussed in the context of structural dynamics. A.I. Gordeyev 2014 /pmc/articles/PMC4207560/ /pubmed/25349714 Text en Copyright ® 2014 Park-media Ltd. http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Koval, V. V.
Knorre, D. G.
Fedorova, O. S.
Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA
title Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA
title_full Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA
title_fullStr Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA
title_full_unstemmed Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA
title_short Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA
title_sort structural features of the interaction between human 8-oxoguanine dna glycosylase hogg1 and dna
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4207560/
https://www.ncbi.nlm.nih.gov/pubmed/25349714
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