Natural protein proteinase inhibitors and their interaction with proteinases

Eur J Biochem. 1992 Mar 1;204(2):433-51. doi: 10.1111/j.1432-1033.1992.tb16654.x.


The substrate-like 'canonical' inhibition by the 'small' serine proteinase inhibitors and the product-like inhibition by the carboxypeptidase inhibitor have provided the only atomic models of protein inhibitor--proteinase interactions for about 15 years. The recently published structures of cystatin/stefin--papain complexes and of hirudin--thrombin complexes reveal novel non-substrate-like interactions. In addition, the structure of pro-carboxypeptidase shows a model of inactivation which bears resemblance to proteinase/protein inhibitor systems. Considerable progress in understanding the transition between native and cleaved states of the serpins has also been made by several recent structural studies.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Carboxypeptidases / antagonists & inhibitors
  • Enzyme Precursors / antagonists & inhibitors
  • Magnetic Resonance Spectroscopy
  • Protease Inhibitors / metabolism*
  • Protein Conformation
  • X-Ray Diffraction


  • Enzyme Precursors
  • Protease Inhibitors
  • Carboxypeptidases