An inhibition model of BPTI to unlinked dengue virus NS2B‐NS3 protease

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  • Hua Li
    Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China
  • Lei Zhu
    High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China
  • Shulin Hou
    Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China
  • Jing Yang
    High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China
  • Junfeng Wang
    High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China
  • Jinsong Liu
    Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China

書誌事項

公開日
2014-06-12
権利情報
  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1016/j.febslet.2014.05.063
公開者
Wiley

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説明

<jats:p>One approach to treating the dengue virus infection is to inhibit its NS2B‐NS3 protease that plays a vital role in virus maturation. However, the lack of structural information on the active conformation of the protease hindered related drug design. With a co‐expression system, we obtained the active two‐component protease in its unlinked form. BPTI shows strong competitive inhibitory activity (<jats:italic>K</jats:italic><jats:sub>i</jats:sub> = 6.5 nM) against this unlinked protease, which adopts a closed conformation. Based on the biochemical and NMR perturbation information, an inhibition model of BPTI to NS2B‐NS3 protease is proposed.</jats:p>

収録刊行物

  • FEBS Letters

    FEBS Letters 588 (17), 2794-2799, 2014-06-12

    Wiley

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