5ABJ

Structure of Coxsackievirus A16 in complex with GPP3

Summary for 5ABJ

• Entry DOI: 10.2210/pdb5abj/pdb
• Descriptor: VP1, VP2, VP3, ... (8 entities in total)
• Functional Keywords: virus, inhibitor
• Biological source: COXSACKIEVIRUS A16; More
• Cellular location: Host cytoplasm : I3W9E1 I3W9E1 I3W9E1 I3W9E1
• Total number of polymer chains: 4
• Total formula weight: 95309.88

Authors

De Colibus, L.,Wang, X.,Tijsma, A.,Neyts, J.,Spyrou, J.A.B.,Ren, J.,Grimes, J.M.,Puerstinger, G.,Leyssen, P.,Fry, E.E.,Rao, Z.,Stuart, D.I. (deposition date: 2015-08-06, release date: 2015-09-09, Last modification date: 2024-05-08)

Primary citation

De Colibus, L.,Wang, X.,Tijsma, A.,Neyts, J.,Spyrou, J.A.B.,Ren, J.,Grimes, J.M.,Puerstinger, G.,Leyssen, P.,Fry, E.E.,Rao, Z.,Stuart, D.I.
Structure Elucidation of Coxsackievirus A16 in Complex with Gpp3 Informs a Systematic Review of Highly Potent Capsid Binders to Enteroviruses.
Plos Pathog., 11:5165-, 2015

PubMed Abstract: The replication of enterovirus 71 (EV71) and coxsackievirus A16 (CVA16), which are the major cause of hand, foot and mouth disease (HFMD) in children, can be inhibited by the capsid binder GPP3. Here, we present the crystal structure of CVA16 in complex with GPP3, which clarifies the role of the key residues involved in interactions with the inhibitor. Based on this model, in silico docking was performed to investigate the interactions with the two next-generation capsid binders NLD and ALD, which we show to be potent inhibitors of a panel of enteroviruses with potentially interesting pharmacological properties. A meta-analysis was performed using the available structural information to obtain a deeper insight into those structural features required for capsid binders to interact effectively and also those that confer broad-spectrum anti-enterovirus activity.

PubMed: 26485389
DOI: 10.1371/JOURNAL.PPAT.1005165

Experimental method

X-RAY DIFFRACTION (2.75 Å)