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-Structure paper
タイトル | Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enteroviruses. |
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ジャーナル・号・ページ | Commun Biol, Vol. 4, Issue 1, Page 250, Year 2021 |
掲載日 | 2021年2月26日 |
著者 | Justin W Flatt / Aušra Domanska / Alma L Seppälä / Sarah J Butcher / |
PubMed 要旨 | 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 ...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. |
リンク | Commun Biol / PubMed:33637854 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.7 - 3.4 Å |
構造データ | EMDB-11165, PDB-6zck: EMDB-11166, PDB-6zcl: EMDB-11300, PDB-6zms: |
化合物 | ChemComp-QFW: ChemComp-FHK: ChemComp-MYR: |
由来 |
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キーワード | VIRUS / Enterovirus / Coxsackievirus B4 / Inhibitor / Capsid Binder / coxackievirus B4 |