Journal articles
Structure of the Respiratory Syncytial Virus Polymerase Complex
Abstract : Graphical Abstract Highlights d Cryo-EM structure of RSV L bound by tetrameric RSV P solved to 3.2 Å d P tetramer adopts an asymmetric tentacular arrangement when bound to L d L priming loop adopts elongation-compatible state without PRNTase-RdRp separation d Structure rationalizes escape from small-molecule antivirals In Brief Respiratory syncytial virus (RSV) remains a leading cause of bronchiolitis and hospitalization, especially of infants. Gilman et al. present a 3.2-Å cryo-EM structure of the RSV L polymerase in complex with the P phosphoprotein-components of the core viral replication machinery that represent an attractive target for the development of therapeutic agents. Data Resources 6PZK
Cited literature [93 references]
https://hal-amu.archives-ouvertes.fr/hal-02353778
Contributor : Etienne Decroly <>
Submitted on : Thursday, November 7, 2019 - 2:26:45 PM
Last modification on : Thursday, December 3, 2020 - 5:12:04 PM
Long-term archiving on: : Sunday, February 9, 2020 - 12:07:04 AM
Contributor : Etienne Decroly <>
Submitted on : Thursday, November 7, 2019 - 2:26:45 PM
Last modification on : Thursday, December 3, 2020 - 5:12:04 PM
Long-term archiving on: : Sunday, February 9, 2020 - 12:07:04 AM
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PIIS009286741930902X.pdf
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