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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
A.I. Gordeyev
2014
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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. |
format | Online Article Text |
id | pubmed-4207560 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | A.I. Gordeyev |
record_format | MEDLINE/PubMed |
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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