Proteinase-protein inhibitor interaction.
Until recently, the "substrate-like" "canonical" inhibition by the "small" serine proteinase inhibitors, and the product-like inhibition by the carboxypeptidase inhibitor, provided the only models for protein inhibitor-proteinase interactions. The recently published structures of cystatin/stefin-papain complexes and of hirudin-thrombin complexes reveal novel modes of interactions of only partial substrate-like character. Despite considerable progress in understanding the native-cleaved transition of the serpins, the mechanisms of their interaction with their cognate serine proteinases is still a matter of conjecture.
Bode
W
W
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Huber
R
R
D000818:Animals; D001665:Binding Sites; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D006629:Hirudins / Q000378:metabolism; D006801:Humans; D015394:Molecular Structure; D011480:Protease Inhibitors / Q000737:chemistry / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism; D015843:Serpins / Q000378:metabolism; D013917:Thrombin / Q000378:metabolism
D006629:Hirudins; D011480:Protease Inhibitors; D015843:Serpins; D010450:Endopeptidases; D012697:Serine Endopeptidases; D013917:Thrombin