Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) macrodomain within the nonstructural protein 3 counteracts host-mediated antiviral adenosine diphosphate–ribosylation signaling. This enzyme is a promising antiviral target because catalytic mutations render viruses nonpathogenic. Here...

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Bibliographic Details
Main Authors:	Schuller, M, Correy, GJ, Gahbauer, S, Fearon, D, Wu, T, Díaz, RE, Young, ID, Carvalho Martins, L, Smith, DH, Schulze-Gahmen, U, Owens, TW, Deshpande, I, Merz, GE, Thwin, AC, Biel, JT, Peters, JK, Moritz, M, Herrera, N, Kratochvil, HT, Aimon, A, Bennett, JM, Brandao Neto, J, Cohen, AE, Dias, A, Douangamath, A, Dunnett, L, Fedorov, O, Ferla, MP, Fuchs, MR, Gorrie-Stone, TJ, Holton, JM, Johnson, MG, Krojer, T, Meigs, G, Powell, AJ, Rack, JGM, Rangel, VL, Russi, S, Skyner, RE, Smith, CA, Soares, AS, Wierman, JL, O'Brien, P, Zhu, K, Jura, N, Ashworth, A, Irwin, JJ, Thompson, MC, Gestwicki, JE, von Delft, F, Ahel, I
Other Authors:	QCRG Structural Biology Consortium
Format:	Journal article
Language:	English
Published:	American Association for the Advancement of Science 2021

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

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