The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase

DNA glycosylases are lesion-specific enzymes that recognize specific nucleobase damages and catalyze their excision through cleavage of the glycosidic bond. Here, the authors present the crystal structures of human 8-oxoguanine (oxoG) DNA glycosylase bound to undamaged DNA and to DNA containing an i...

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Autores principales:	Uddhav K. Shigdel, Victor Ovchinnikov, Seung-Joo Lee, Jenny A. Shih, Martin Karplus, Kwangho Nam, Gregory L. Verdine
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/60b39eb87d0b47c4a0f3eab9bd903e6e
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spelling	oai:doaj.org-article:60b39eb87d0b47c4a0f3eab9bd903e6e2021-12-02T19:12:29ZThe trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase10.1038/s41467-020-18290-22041-1723https://doaj.org/article/60b39eb87d0b47c4a0f3eab9bd903e6e2020-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18290-2https://doaj.org/toc/2041-1723DNA glycosylases are lesion-specific enzymes that recognize specific nucleobase damages and catalyze their excision through cleavage of the glycosidic bond. Here, the authors present the crystal structures of human 8-oxoguanine (oxoG) DNA glycosylase bound to undamaged DNA and to DNA containing an intrahelical oxoG lesion and further analyse these structures with molecular dynamics simulations, which allows them to characterise the base-extrusion pathways.Uddhav K. ShigdelVictor OvchinnikovSeung-Joo LeeJenny A. ShihMartin KarplusKwangho NamGregory L. VerdineNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-8 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Uddhav K. Shigdel Victor Ovchinnikov Seung-Joo Lee Jenny A. Shih Martin Karplus Kwangho Nam Gregory L. Verdine The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
description	DNA glycosylases are lesion-specific enzymes that recognize specific nucleobase damages and catalyze their excision through cleavage of the glycosidic bond. Here, the authors present the crystal structures of human 8-oxoguanine (oxoG) DNA glycosylase bound to undamaged DNA and to DNA containing an intrahelical oxoG lesion and further analyse these structures with molecular dynamics simulations, which allows them to characterise the base-extrusion pathways.
format	article
author	Uddhav K. Shigdel Victor Ovchinnikov Seung-Joo Lee Jenny A. Shih Martin Karplus Kwangho Nam Gregory L. Verdine
author_facet	Uddhav K. Shigdel Victor Ovchinnikov Seung-Joo Lee Jenny A. Shih Martin Karplus Kwangho Nam Gregory L. Verdine
author_sort	Uddhav K. Shigdel
title	The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_short	The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_full	The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_fullStr	The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_full_unstemmed	The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase
title_sort	trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine dna glycosylase
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/60b39eb87d0b47c4a0f3eab9bd903e6e
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The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase

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