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Scientific reports v.6, 2016년, pp.37539 -    SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Product release is rate-limiting for catalytic processing by the Dengue virus protease

Shannon, A. E. (School of Chemistry and Molecular Biosciences, University of Queensland, St Lucia, Queensland 4072, Australia ) ; Pedroso, M. M. (School of Chemistry and Molecular Biosciences, University of Queensland, St Lucia, Queensland 4072, Australia ) ; Chappell, K. J. (School of Chemistry and Molecular Biosciences, University of Queensland, St Lucia, Queensland 4072, Australia ) ; Watterson, D. (School of Chemistry and Molecular Biosciences, University of Queensland, St Lucia, Queensland 4072, Australia ) ; Liebscher, S. (School of Chemistry and Molecular Biosciences, University of Queensland, St Lucia, Queensland 4072, Australia ) ; Kok, W. M. (ARC Centre of Excellence in Advanced Molecular Imaging, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia ) ; Fairlie, D. P. (ARC Centre of Excellence in Advanced Molecular Imaging, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia ) ; Schenk, G. (School of Chemistry and Molecular Biosciences, University of Queensland, St Lucia, Queensland 4072, Australia ) ; Young, P. R. (ARC Centre of ) ;
  • 초록  

    Dengue Virus (DENV) is the most prevalent global arbovirus, yet despite an increasing burden to health care there are currently no therapeutics available to treat infection. A potential target for antiviral drugs is the two-component viral protease NS2B-NS3pro, which is essential for viral replication. Interactions between the two components have been investigated here by probing the effect on the rate of enzyme catalysis of key mutations in a mobile loop within NS2B that is located at the interface of the two components. Steady-state kinetic assays indicated that the mutations greatly affect catalytic turnover. However, single turnover and fluorescence experiments have revealed that the mutations predominantly affect product release rather than substrate binding. Fluorescence analysis also indicated that the addition of substrate triggers a near-irreversible change in the enzyme conformation that activates the catalytic centre. Based on this mechanistic insight, we propose that residues within the mobile loop of NS2B control product release and present a new target for design of potent Dengue NS2B-NS3 protease inhibitors.


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