5DP5

Crystal Structure of EV71 3C Proteinase in complex with compound 4

Summary for 5DP5

• Entry DOI: 10.2210/pdb5dp5/pdb
• Related: 5DP3 5DP4 5DP6 5DP7 5DP8 5DP9 5DPA
• Descriptor: 3C proteinase, ethyl (2Z,4S)-4-{[(2R,5S)-5-amino-2-(4-fluorobenzyl)-6-methyl-4-oxoheptanoyl]amino}-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate (3 entities in total)
• Functional Keywords: hand, foot and mouth disease, 3c proteinase, peptidomimetics, drug design, rupintrivir, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Enterovirus A71
• Cellular location: Host cytoplasm : A9XG43
• Total number of polymer chains: 1
• Total formula weight: 20465.59

Authors

Wu, C.,Zhang, L.,Li, P.,Cai, Q.,Peng, X.,Li, N.,Cai, Y.,Li, J.,Lin, T. (deposition date: 2015-09-12, release date: 2016-03-30, Last modification date: 2016-04-06)

Primary citation

Wu, C.,Zhang, L.,Li, P.,Cai, Q.,Peng, X.,Yin, K.,Chen, X.,Ren, H.,Zhong, S.,Weng, Y.,Guan, Y.,Chen, S.,Wu, J.,Li, J.,Lin, T.
Fragment-wise design of inhibitors to 3C proteinase from enterovirus 71
Biochim.Biophys.Acta, 1860:1299-1307, 2016

PubMed Abstract: Enterovirus 71 (EV71) is a causative agent of hand, foot and mouth disease (HFMD), which can spread its infection to central nervous and other systems with severe consequence. A key factor in the replication of EV71 is its 3C proteinase (3C(pro)), a significant drug target. Peptidomimetics were employed as inhibitors of this enzyme for developing antivirals. However, the peptide bonds in these peptidomimetics are a source of low bioavailability due to their susceptibility to protease digestion. To produce non-peptidomimetic inhibitors by replacing these peptide bonds, it would be important to gain better understanding on the contribution of each component to the interaction and potency.

PubMed: 26987809
DOI: 10.1016/j.bbagen.2016.03.017

Experimental method

X-RAY DIFFRACTION (2.03 Å)