title: Natural protein proteinase inhibitors and their interaction with proteinases.
abstract: 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.
authors.affiliation: Max-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
authors.forename: W
authors.initials: W
authors.lastname: Bode
authors.forename: R
authors.initials: R
authors.lastname: Huber
mesh_terms: D000818:Animals; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors; D009682:Magnetic Resonance Spectroscopy; D011480:Protease Inhibitors / Q000378:metabolism*; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D004792:Enzyme Precursors; D011480:Protease Inhibitors; D002268:Carboxypeptidases