Endoproteinase-protein inhibitor interactions.
Nature uses protein inhibitors as important tools to regulate the proteolytic activity of their target proteinases. Most of these inhibitors for which 3D structures are available are directed towards serine proteinases, interacting with their active-sites in a substrate-like "canonical" manner via an exposed reactive-site loop of conserved conformation. More recently, some non-canonically binding serine proteinase inhibitors, two cysteine proteinase inhibitors, and three zinc endopeptidase inhibitors have been characterized in the free and complexed state, displaying novel mechanisms of inhibition with their target proteinases. These different interaction modes are briefly discussed, with particular emphasis on the interaction between matrix metalloproteinases (MMPs) and their endogenous tissue inhibitors of metalloproteinases (TIMPs).
Bode
W
W
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Fernandez-Catalan
C
C
Nagase
H
H
Maskos
K
K
D000818:Animals; D001665:Binding Sites; D015891:Cystatins / Q000737:chemistry; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry*; D010450:Endopeptidases / Q000737:chemistry*; D006801:Humans; D019476:Insect Proteins / Q000737:chemistry; D019278:Matrix Metalloproteinase 3 / Q000737:chemistry; D015842:Serine Proteinase Inhibitors / Q000737:chemistry*; D019715:Tissue Inhibitor of Metalloproteinase-1 / Q000737:chemistry*
D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D019476:Insect Proteins; D015842:Serine Proteinase Inhibitors; D019715:Tissue Inhibitor of Metalloproteinase-1; C082506:rhodniin protein, Rhodnius; D010450:Endopeptidases; D019278:Matrix Metalloproteinase 3