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- W86660412 abstract "Publisher Summary This chapter examines the structural chemistry and the biological aspects of Matrix metalloproteinase 21 (XMMP). The sequence of XMMP contains 604 amino acids including a putative signal peptide of 22 residues with a characteristic hydropathy profile. There are no other significant hydrophobic segments, suggesting that XMMP is a secretory protein. At the end of the propeptide, after the cysteine switch PRCGVPD motif, XMMP has a 37 amino acid insertion domain followed by a putative cleavage site for intracellular activation by furin proteinases. The catalytic domain has a unique cysteine; an insertion in a sequence motif that binds the structural zinc in MMPs. XMMP lacks a proline-rich linker peptide or a hinge region that is typically found in other MMPs between the catalytic domain and C-terminal hemopexin/vitronectin like domain. The linker peptide is the most variable region of MMPs, and plays a role in MMP activity and substrate specificity. XMMP has a calculated molecular weight of 70115 and a catalytically active form 47072. The sequence of XMMP is significantly different from other MMPs. It is found that in a phylogenetic tree of MMPs, XMMP is at the very bottom, providing an outlier from which the branching and MMP evolution begins." @default.
- W86660412 created "2016-06-24" @default.
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- W86660412 date "2004-01-01" @default.
- W86660412 modified "2023-10-16" @default.
- W86660412 title "Matrix metalloproteinase 21" @default.
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- W86660412 doi "https://doi.org/10.1016/b978-0-12-079611-3.50153-1" @default.
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