6KU7

structure of HRV-C 3C protein

Summary for 6KU7

• Entry DOI: 10.2210/pdb6ku7/pdb
• Descriptor: Genome polyprotein (2 entities in total)
• Functional Keywords: hrv, 3c, protease, hydrolase
• Biological source: Rhinovirus C
• Total number of polymer chains: 1
• Total formula weight: 20891.73

Authors

Zhu, L.,Yuan, S. (deposition date: 2019-08-31, release date: 2020-03-25, Last modification date: 2023-11-22)

Primary citation

Yuan, S.,Fan, K.,Chen, Z.,Sun, Y.,Hou, H.,Zhu, L.
Structure of the HRV-C 3C-Rupintrivir Complex Provides New Insights for Inhibitor Design.
Virol Sin, 35:445-454, 2020

PubMed Abstract: Human rhinoviruses (HRVs) are the predominant infectious agents for the common cold worldwide. The HRV-C species cause severe illnesses in children and are closely related to acute exacerbations of asthma. 3C protease, a highly conserved enzyme, cleaves the viral polyprotein during replication and assists the virus in escaping the host immune system. These key roles make 3C protease an important drug target. A few structures of 3Cs complexed with an irreversible inhibitor rupintrivir have been determined. These structures shed light on the determinants of drug specificity. Here we describe the structures of HRV-C15 3C in free and inhibitor-bound forms. The volume-decreased S1' subsite and half-closed S2 subsite, which were thought to be unique features of enterovirus A 3C proteases, appear in the HRV-C 3C protease. Rupintrivir assumes an "intermediate" conformation in the complex, which might open up additional avenues for the design of potent antiviral inhibitors. Analysis of the features of the three-dimensional structures and the amino acid sequences of 3C proteases suggest new applications for existing drugs.

PubMed: 32103448
DOI: 10.1007/s12250-020-00196-4

Experimental method

X-RAY DIFFRACTION (2.15 Å)