elastin + H2O |
degradation. MMP-7 mainly cleaves in N- and C-terminal regions of elastin's precursor, which involves linkages in domains encoded by exons 2, 3, 5-7, 26, and 30-33. Only few cleavages occur in the central part of the precursor and no cleavages in regions in elastin that are involved in cross-linking. MMP-7 shows a strong preference for Leu in P1' and also accepts Val, Gly, and Pro at this position, whereas Ala is not preferred at P1', molecular modeling, overview. Not only the size of the amino acid residue in P1' but also the orientation of the neighboring P1 residue and, thus, the orientation of the peptide bond that is cleaved influences the cleavage preference of MMP-7, cleavage site specificity of MMP-7 in human skin elastin, overview |
Homo sapiens |
elastin peptides |
in the range of 500-8000 Da |
? |
|
additional information |
two substrate peptides present in human skin elastin: PGGLAG, residues 67-72, containing Leu at P1', and LGGAGQ, residues 754-759, containing Ala at P1', and two further peptides PGGAAG and PGGGAG are modeled and docked into the MMP-7 catalytic site. The binding site was defined on the zinc ion |
Homo sapiens |
? |
- |
? |
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