6ZCK
Coxsackievirus B4 in complex with capsid binder compound 48
Summary for 6ZCK
Entry DOI | 10.2210/pdb6zck/pdb |
EMDB information | 11165 |
Descriptor | Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (5 entities in total) |
Functional Keywords | enterovirus, coxsackievirus b4, inhibitor, capsid binder, virus |
Biological source | Coxsackievirus B4 (strain E2) More |
Total number of polymer chains | 4 |
Total formula weight | 92722.40 |
Authors | Flatt, J.W.,Domanska, A.,Butcher, S.J. (deposition date: 2020-06-11, release date: 2021-03-17, Last modification date: 2024-07-10) |
Primary citation | Flatt, J.W.,Domanska, A.,Seppala, A.L.,Butcher, S.J. Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enteroviruses. Commun Biol, 4:250-250, 2021 Cited by PubMed Abstract: Enteroviruses pose a persistent and widespread threat to human physical health, with no specific treatments available. Small molecule capsid binders have the potential to be developed as antivirals that prevent virus attachment and entry into host cells. To aid with broad-range drug development, we report here structures of coxsackieviruses B3 and B4 bound to different interprotomer-targeting capsid binders using single-particle cryo-EM. The EM density maps are beyond 3 Å resolution, providing detailed information about interactions in the ligand-binding pocket. Comparative analysis revealed the residues that form a conserved virion-stabilizing network at the interprotomer site, and showed the small molecule properties that allow anchoring in the pocket to inhibit virus disassembly. PubMed: 33637854DOI: 10.1038/s42003-021-01779-x PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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