Structural Insights into Binding of Remdesivir Triphosphate within the Replication–Transcription Complex of SARS-CoV-2

Autor:	Jimin Wang, Yuanjun Shi, Krystle Reiss, Federica Maschietto, Elias Lolis, William H. Konigsberg, George P. Lisi, Victor S. Batista
Rok vydání:	2022
Předmět:	Adenosine Triphosphate Alanine Coronavirus RNA-Dependent RNA Polymerase Nucleotides SARS-CoV-2 Deoxyribonucleotides RNA Viral Ribonucleotides Antiviral Agents Biochemistry Adenosine Monophosphate Hydrogen COVID-19 Drug Treatment
Zdroj:	Biochemistry. 61:1966-1973
ISSN:	1520-4995 0006-2960
Popis:	Remdesivir is an adenosine analogue that has a cyano substitution in the C1' position of the ribosyl moiety and a modified base structure to stabilize the linkage of the base to the C1' atom with its strong electron-withdrawing cyano group. Within the replication-transcription complex (RTC) of SARS-CoV-2, the RNA-dependent RNA polymerase nsp12 selects remdesivir monophosphate (RMP) over adenosine monophosphate (AMP) for nucleotide incorporation but noticeably slows primer extension after the added RMP of the RNA duplex product is translocated by three base pairs. Cryo-EM structures have been determined for the RTC with RMP at the nucleotide-insertion (
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6296e0f3d24eb8b117db2d90b346328 https://doi.org/10.1021/acs.biochem.2c00341 Zobrazit plný text záznamu