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Substrate Specificities of Matrix Metalloproteinase 1 in PAR‐1 Exodomain Proteolysis
Author(s) -
Nesi Antonella,
Fragai Marco
Publication year - 2007
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700055
Subject(s) - proteolysis , cleavage (geology) , matrix metalloproteinase , metalloproteinase , chemistry , substrate specificity , biochemistry , substrate (aquarium) , extracellular matrix , extracellular , agonist , receptor , enzyme , stereochemistry , microbiology and biotechnology , biology , ecology , paleontology , fracture (geology)
Hydrophobic sites preferred . The proteolysis of the extracellular domain of the G protein‐coupled proteinase‐activated receptor 1 (PAR‐1) by matrix metalloproteinase 1 (MMP‐1) has been investigated by NMR spectroscopy and MS. The different specificity of MMP‐1 agonist thrombin with respect to the natural, and the identification of a cleavage site within the functional hexapeptide provide new insight on the molecular bases of PAR‐1 activation by MMP‐1.