Substrate specificities of matrix metalloproteinase 1 in PAR-1 exodomain proteolysis

被引：17

作者：

Nesi, Antonella

Fragai, Marco

机构：

[1] Univ Florence, Magnet Resonance Ctr, I-50019 Florence, Italy

[2] Univ Florence, Dept Agr Biotechnol, I-50144 Florence, Italy

来源：

CHEMBIOCHEM | 2007年 / 8卷 / 12期

关键词：

enzymes; mass spectroscopy; metalloproteases; NMR spectroscopy; receptors;

D O I：

10.1002/cbic.200700055

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

(Figure Presented) 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. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

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页码：1367 / 1369

页数：3

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