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March 1, 1997Journal of VirologyOpen Access

The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition

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Authors

EBE.M. BergmannUniversity Hospital Bonn SMS.C. MosimannMedical Council of Canada MCMaia M. ChernaiaEngelhardt Institute of Molecular Biology

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Implication

HAV 3C proteinase structure now solved; leaves open structure-based antiviral design pending functional studies.

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Key points are not available for this paper at this time.

Cite This Study

Bergmann et al. (1997) studied this question.

synapsesocial.com/papers/6a7fbcfb6d8c9e2704ec9efb https://doi.org/10.1128/jvi.71.3.2436-2448.1997

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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1A rapid method for determination of endoproteinase substrate specificity: specificity of the 3C proteinase from hepatitis A virus.1991 · 47 citations
2Human rhinovirus-14 protease 3C (3Cpro) binds specifically to the 5'-noncoding region of the viral RNA. Evidence that 3Cpro has different domains for the RNA binding and proteolytic activities.1993 · 89 citations
3Complete nucleotide sequence of wild-type hepatitis A virus: comparison with different strains of hepatitis A virus and other picornaviruses1987 · 385 citations
4Expression and site-specific mutagenesis of the poliovirus 3C protease in Escherichia coli.1986 · 96 citations
5Stimulation of poliovirus proteinase 3Cpro-related proteolysis by the genome-linked protein VPg and its precursor 3AB.1994 · 100 citations