Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex

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Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complexChen et al. present cryo-EM structures of the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) holoenzyme (nsp7/nsp8/nsp12) containing an RNA template-product in complex with the viral helicase (nsp13). The work provides insight into the assembly and function of the multi-subunit protein machine and how it might be targeted therapeutically to treat COVID-19.Chen et al. present cryo-EM structures of the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) holoenzyme (nsp7/nsp8/nsp12) containing an RNA template-product in complex with the viral helicase (nsp13). The work provides insight into the assembly and function of the multi-subunit protein machine and how it might be targeted therapeutically to treat COVID-19.James Chen, Brandon Malone, Eliza Llewellyn, Michael Grasso, Patrick M.M. Shelton, Paul Dominic B. Olinares, Kashyap Maruthi, Ed T. Eng, Hasan Vatandaslar, Brian T. Chait, Tarun Kapoor, Seth A. Darst, Elizabeth A. Campbellhttps://secure.jbs.elsevierhealth.com/action/getSharedSiteSession?redirect=https%3A%2F%2Fwww.cell.com%2Fcell%2Ffulltext%2FS0092-8674%2820%2930941-7%3Frss%3Dyes&rc=0http://www.cell.com/cell/inpress.rssCellCell RSS feed.Wireless News CampaignJuly 29, 2020

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