ArticlePloS one2012
Structure of a murine norovirus NS6 protease-product complex revealed by adventitious crystallisation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Thrombin cleavage of the hepatitis E virus polyprotein at multiple conserved locations is required for genome replication.PLoS pathogens · 2023Article
- Norovirus Protease Structure and Antivirals Development.Viruses · 2021Review
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- Structural and Antiviral Studies of the Human Norovirus GII.4 Protease.Biochemistry · 2019Article
- Selection and Characterization of Rupintrivir-Resistant Norwalk Virus Replicon CellsAntimicrobial agents and chemotherapy · 2018Article
- Structure and Function of Caliciviral RNA Polymerases.Viruses · 2017Review
- Antiviral targets of human noroviruses.Current opinion in virology · 2016Review
- Current tools for norovirus drug discovery.Expert opinion on drug discovery · 2016Review
- A Conserved Interaction between a C-Terminal Motif in Norovirus VPg and the HEAT-1 Domain of eIF4G Is Essential for Translation Initiation.PLoS pathogens · 2016Article
- A Cell-based Fluorescence Resonance Energy Transfer (FRET) Sensor Reveals Inter- and Intragenogroup Variations in Norovirus Protease Activity and Polyprotein Cleavage.The Journal of biological chemistry · 2015Article
- Article
- Structure-based design and functional studies of novel noroviral 3C protease chimaeras offer insights into substrate specificity.The Biochemical journal · 2014Article
- The p4-p2' amino acids surrounding human norovirus polyprotein cleavage sites define the core sequence regulating self-processing order.Journal of virology · 2014Article
- The enterovirus protease inhibitor rupintrivir exerts cross-genotypic anti-norovirus activity and clears cells from the norovirus replicon.Antimicrobial agents and chemotherapy · 2014Article
- Structural and inhibitor studies of norovirus 3C-like proteases.Virus research · 2013Article
- Structural basis of substrate specificity and protease inhibition in Norwalk virus.Journal of virology · 2013Article
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Murine noroviruses have emerged as a valuable tool for investigating the molecular basis of infection and pathogenesis of the closely related human noroviruses, which are the major cause of non-bacterial gastroenteritis. The replication of noroviruses relies on the proteolytic processing of a large polyprotein precursor into six non-structural proteins (NS1-2, NS3, NS4, NS5, NS6(pro), NS7(pol)) by the virally-encoded NS6 protease. We report here the crystal structure of MNV NS6(pro), which has been determined to a resolution of 1.6 Å. Adventitiously, the crystal contacts are mediated in part by the binding of the C-terminus of NS6(pro) within the peptide-binding cleft of a neighbouring molecule. This insertion occurs for both molecules in the asymmetric unit of the crystal in a manner that is consistent with physiologically-relevant binding, thereby providing two independent views of a protease-peptide complex. Since the NS6(pro) C-terminus is formed in vivo by NS6(pro) processing, these crystal contacts replicate the protease-product complex that is formed immediately following cleavage of the peptide bond at the NS6-NS7 junction. The observed mode of binding of the C-terminal product peptide yields new insights into the structural basis of NS6(pro) specificity.
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