Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase

Various herpesvirus therapeutics target the viral DNA polymerase. Here, the authors present the crystal structure of herpesvirus polymerase in the elongating state with bound primer-template DNA and the broad-spectrum non-nucleoside inhibitor PNU-183792, which is of interest for further drug design.

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Autores principales:	Robert P. Hayes, Mee Ra Heo, Mark Mason, John Reid, Christine Burlein, Kira A. Armacost, David M. Tellers, Izzat Raheem, Anthony W. Shaw, Edward Murray, Philip M. McKenna, Pravien Abeywickrema, Sujata Sharma, Stephen M. Soisson, Daniel Klein
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/4bd96a2415b244b397a96da4a23966c4
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spelling	oai:doaj.org-article:4bd96a2415b244b397a96da4a23966c42021-12-02T14:42:18ZStructural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase10.1038/s41467-021-23312-82041-1723https://doaj.org/article/4bd96a2415b244b397a96da4a23966c42021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23312-8https://doaj.org/toc/2041-1723Various herpesvirus therapeutics target the viral DNA polymerase. Here, the authors present the crystal structure of herpesvirus polymerase in the elongating state with bound primer-template DNA and the broad-spectrum non-nucleoside inhibitor PNU-183792, which is of interest for further drug design.Robert P. HayesMee Ra HeoMark MasonJohn ReidChristine BurleinKira A. ArmacostDavid M. TellersIzzat RaheemAnthony W. ShawEdward MurrayPhilip M. McKennaPravien AbeywickremaSujata SharmaStephen M. SoissonDaniel KleinNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-7 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Robert P. Hayes Mee Ra Heo Mark Mason John Reid Christine Burlein Kira A. Armacost David M. Tellers Izzat Raheem Anthony W. Shaw Edward Murray Philip M. McKenna Pravien Abeywickrema Sujata Sharma Stephen M. Soisson Daniel Klein Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase
description	Various herpesvirus therapeutics target the viral DNA polymerase. Here, the authors present the crystal structure of herpesvirus polymerase in the elongating state with bound primer-template DNA and the broad-spectrum non-nucleoside inhibitor PNU-183792, which is of interest for further drug design.
format	article
author	Robert P. Hayes Mee Ra Heo Mark Mason John Reid Christine Burlein Kira A. Armacost David M. Tellers Izzat Raheem Anthony W. Shaw Edward Murray Philip M. McKenna Pravien Abeywickrema Sujata Sharma Stephen M. Soisson Daniel Klein
author_facet	Robert P. Hayes Mee Ra Heo Mark Mason John Reid Christine Burlein Kira A. Armacost David M. Tellers Izzat Raheem Anthony W. Shaw Edward Murray Philip M. McKenna Pravien Abeywickrema Sujata Sharma Stephen M. Soisson Daniel Klein
author_sort	Robert P. Hayes
title	Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase
title_short	Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase
title_full	Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase
title_fullStr	Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase
title_full_unstemmed	Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase
title_sort	structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/4bd96a2415b244b397a96da4a23966c4
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Structural understanding of non-nucleoside inhibition in an elongating herpesvirus polymerase

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