Morrissey Lab, University of Michigan
  • 8/2025 Our cryo-EM structure of the membrane-bound tissue factor/factor VIIa complex with a
    factor X mimetic is now published in Blood
    , revealing how the trimolecular complex that
    triggers blood clotting in both normal hemostasis and many thrombotic diseases
    assembles on a membrane surface. This structure now provides a clear mechanistic
    explanation for more than 30 years’ worth of biochemical studies about tissue factor’s
    substrate-binding “exosite.” It also reveals a novel, membrane-dependent allosteric
    activation mechanism to explain the otherwise puzzling phenomenon of
    encryption/decryption of cell-surface tissue factor. This study was a highly rewarding
    collaboration between the labs of James Morrissey, Melanie Ohi, and Michael
    Cianfrocco at the University of Michigan, and Emad Tajkhorshid’s group at the
    University of Illinois.