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.
Substrate specificities of matrix metalloproteinase 1 in PAR-1 exodomain proteolysis / A. Nesi; M. Fragai. - In: CHEMBIOCHEM. - ISSN 1439-4227. - STAMPA. - 8:(2007), pp. 1367-1369. [10.1002/cbic.200700055]
Substrate specificities of matrix metalloproteinase 1 in PAR-1 exodomain proteolysis
NESI, ANTONELLA;FRAGAI, MARCO
2007
Abstract
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.
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