Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site

The major product of oxidative base damage is 8-oxo-7,8-dihydro-2′-deoxyguanine (8odG). The coding potential of this lesion is modulated by its glycosidic torsion angle that controls whether its Watson-Crick or Hoogsteen edge is utilized for base pairing. The 2.0 Å structure of DNA polymerase (pol)...

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Autores principales: Batra, Vinod K., Beard, William A., Hou, Esther W., Pedersen, Lars C., Prasad, Rajendra, Wilson, Samuel H.
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2921931/
https://www.ncbi.nlm.nih.gov/pubmed/20526335
http://dx.doi.org/10.1038/nsmb.1852
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author Batra, Vinod K.
Beard, William A.
Hou, Esther W.
Pedersen, Lars C.
Prasad, Rajendra
Wilson, Samuel H.
author_facet Batra, Vinod K.
Beard, William A.
Hou, Esther W.
Pedersen, Lars C.
Prasad, Rajendra
Wilson, Samuel H.
author_sort Batra, Vinod K.
collection PubMed
description The major product of oxidative base damage is 8-oxo-7,8-dihydro-2′-deoxyguanine (8odG). The coding potential of this lesion is modulated by its glycosidic torsion angle that controls whether its Watson-Crick or Hoogsteen edge is utilized for base pairing. The 2.0 Å structure of DNA polymerase (pol) β bound with 8odGTP opposite template adenine indicates that the modified nucleotide assumes the mutagenic syn-conformation and that the non-mutagenic anti-conformation would be incompatible with efficient DNA synthesis.
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spelling pubmed-29219312011-01-01 Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site Batra, Vinod K. Beard, William A. Hou, Esther W. Pedersen, Lars C. Prasad, Rajendra Wilson, Samuel H. Nat Struct Mol Biol Article The major product of oxidative base damage is 8-oxo-7,8-dihydro-2′-deoxyguanine (8odG). The coding potential of this lesion is modulated by its glycosidic torsion angle that controls whether its Watson-Crick or Hoogsteen edge is utilized for base pairing. The 2.0 Å structure of DNA polymerase (pol) β bound with 8odGTP opposite template adenine indicates that the modified nucleotide assumes the mutagenic syn-conformation and that the non-mutagenic anti-conformation would be incompatible with efficient DNA synthesis. 2010-06-06 2010-07 /pmc/articles/PMC2921931/ /pubmed/20526335 http://dx.doi.org/10.1038/nsmb.1852 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Batra, Vinod K.
Beard, William A.
Hou, Esther W.
Pedersen, Lars C.
Prasad, Rajendra
Wilson, Samuel H.
Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site
title Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site
title_full Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site
title_fullStr Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site
title_full_unstemmed Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site
title_short Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site
title_sort mutagenic conformation of 8-oxo-7,8-dihydro-2′-dgtp in the confines of a dna polymerase active site
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2921931/
https://www.ncbi.nlm.nih.gov/pubmed/20526335
http://dx.doi.org/10.1038/nsmb.1852
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