Skip to main navigation Skip to search Skip to main content

Crystal structure of zika virus ns2b-ns3 protease in complex with a boronate inhibitor

  • Jian Lei
  • , Guido Hansen
  • , Christoph Nitsche
  • , Christian D. Klein
  • , Linlin Zhang
  • , Rolf Hilgenfeld*
  • *Corresponding author for this work

    Research output: Contribution to journal › Article › peer-review

    332 Citations (Scopus)

    Abstract

    The ongoing Zika virus (ZIKV) outbreak is linked to severe neurological disorders. ZIKV relies on its NS2B/NS3 protease for polyprotein processing; hence, this enzyme is an attractive drug target.The 2.7 angstrom crystal structure of ZIKV protease in complex with a peptidomimetic boronic acid inhibitor reveals a cyclic diester between the boronic acid and glycerol. The P2 4- Aminomethylphenylalanine moiety of the inhibitor forms a salt-bridge with the nonconserved Asp83 of NS2B; ion-pairing between Asp83 and the P2 residue of the substrate likely accounts for the enzyme's high catalytic efficiency. The unusual dimer of the ZIKV protease:inhibitor complex seen in the crystal may provide a model for assemblies formed at high local concentrations of protease at the endoplasmatic reticulum membrane, the site of polyprotein processing.

    Original languageEnglish
    Pages (from-to)503-505
    Number of pages3
    JournalScience
    Volume353
    Issue number6298
    DOIs
    Publication statusPublished - 29 Jul 2016

    Fingerprint

    Dive into the research topics of 'Crystal structure of zika virus ns2b-ns3 protease in complex with a boronate inhibitor'. Together they form a unique fingerprint.

    Cite this