About: Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease

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About: Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease
Creator	Walsh, Martin Jones, S Waring, Michael Wild, Aimon, Anthony Brandaõ-Neto, José Carbery, Anna Conor, Davison, Gemma Dias, Alexandre Douangamath, Alice Downes, Dunnett, Louise Fairhead, Michael Fearon, Daren Firth, James Gehrtz, Paul Keely, Aaron Keserü, György Klein, Hanna Krojer, Tobias London, Nir Lukacik, Petra Martin, Mathew Noble, Martin O'brien, Peter Owen, David Powell, Ailsa Reddi, Rambabu Resnick, Efrat Skyner, Rachael Snee, Matthew Strain-Damerell, Claire Von Delft, Frank
Source	BioRxiv
abstract	COVID-19, caused by SARS-CoV-2, lacks effective therapeutics. Additionally, no antiviral drugs or vaccines were developed against the closely related coronavirus, SARS-CoV-1 or MERS-CoV, despite previous zoonotic outbreaks. To identify starting points for such therapeutics, we performed a large-scale screen of electrophile and non-covalent fragments through a combined mass spectrometry and X-ray approach against the SARS-CoV-2 main protease, one of two cysteine viral proteases essential for viral replication. Our crystallographic screen identified 71 hits that span the entire active site, as well as 3 hits at the dimer interface. These structures reveal routes to rapidly develop more potent inhibitors through merging of covalent and non-covalent fragment hits; one series of low-reactivity, tractable covalent fragments was progressed to discover improved binders. These combined hits offer unprecedented structural and reactivity information for on-going structure-based drug design against SARS-CoV-2 main protease.
has issue date	2020-05-27(xsd:dateTime)
bibo:doi	10.1101/2020.05.27.118117
has license	biorxiv
sha1sum (hex)	36b0dbb77b20cf42bf809a0638f0e07a6a54bd0b
schema:url	https://doi.org/10.1101/2020.05.27.118117
resource representing a document's title	Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease
schema:publication	bioRxiv
resource representing a document's body	covid:36b0dbb77b20cf42bf809a0638f0e07a6a54bd0b#body_text
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