7GQ1
PanDDA analysis group deposition -- Crystal Structure of Enterovirus D68 3C Protease in complex with Z166605460
Summary for 7GQ1
| Entry DOI | 10.2210/pdb7gq1/pdb |
| Group deposition | PanDDA analysis group deposition (G_1002271) |
| Descriptor | Protease 3C, thiophene-3-carboxylic acid (3 entities in total) |
| Functional Keywords | diamond i04-1 fragment screening, pandda, xchemexplorer, xce, viral protease, 3c, viral protein |
| Biological source | Human Enterovirus D68 |
| Total number of polymer chains | 2 |
| Total formula weight | 40636.47 |
| Authors | Lithgo, R.M.,Fairhead, M.,Koekemoer, L.,Aschenbrenner, J.C.,Balcomb, B.H.,Godoy, A.S.,Marples, P.G.,Ni, X.,Tomlinson, C.W.E.,Thompson, W.,Wild, C.,Fearon, D.,Walsh, M.A.,von Delft, F. (deposition date: 2023-08-24, release date: 2023-11-29, Last modification date: 2024-10-16) |
| Primary citation | Lithgo, R.M.,Tomlinson, C.W.E.,Fairhead, M.,Winokan, M.,Thompson, W.,Wild, C.,Aschenbrenner, J.C.,Balcomb, B.H.,Marples, P.G.,Chandran, A.V.,Golding, M.,Koekemoer, L.,Williams, E.P.,Wang, S.,Ni, X.,MacLean, E.,Giroud, C.,Godoy, A.S.,Xavier, M.A.,Walsh, M.,Fearon, D.,von Delft, F. Crystallographic Fragment Screen of Coxsackievirus A16 2A Protease identifies new opportunities for the development of broad-spectrum anti-enterovirals. Biorxiv, 2024 Cited by PubMed Abstract: are the causative agents of paediatric hand-foot-and-mouth disease, and a target for pandemic preparedness due to the risk of higher order complications in a large-scale outbreak. The 2A protease of these viruses is responsible for the self-cleavage of the poly protein, allowing for correct folding and assembly of capsid proteins in the final stages of viral replication. These 2A proteases are highly conserved between species, such as . Inhibition of the 2A protease deranges capsid folding and assembly, preventing formation of mature virions in host cells and making the protease a valuable target for antiviral activity. Herein, we describe a crystallographic fragment screening campaign that identified 75 fragments which bind to the 2A protease including 38 unique compounds shown to bind within the active site. These fragments reveal a path for the development of non-peptidomimetic inhibitors of the 2A protease with broad-spectrum anti-enteroviral activity. PubMed: 38746446DOI: 10.1101/2024.04.29.591684 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.32 Å) |
Structure validation
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