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Endoproteinase‐protein inhibitor interactions
Author(s) -
BODE WOLFRAM,
FERNANDEZCATALAN CARLOS,
NAGASE HIDEAKI,
MASKOS KLAUS
Publication year - 1999
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1999.tb01520.x
Subject(s) - serine proteinase inhibitors , matrix metalloproteinase , serine , biochemistry , chemistry , enzyme , endopeptidase , cysteine , proteolysis , binding site , cysteine proteinase inhibitors , active site , serine protease , protease , apoptosis , programmed cell death , caspase
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).