The interaction of MMP-12 with its natural substrate elastin has been characterized by NMR spectroscopy (see figure). The catalytic domain of the full-length protein is most affected, with some involvement also of the hemopexin domain. The interaction is largely maintained in the isolated catalytic domain and involves the active site crevice of the protein and 8–11 elastin residues.
Characterization of the MMP-12-elastin adduct / I.Bertini; M.Fragai; C.Luchinat; M.Melikian; C.Venturi. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - STAMPA. - 15:(2009), pp. 7842-7845. [10.1002/chem.200901009]
Characterization of the MMP-12-elastin adduct
BERTINI, IVANO;FRAGAI, MARCO;LUCHINAT, CLAUDIO;MELIKIAN, MAXIME THIERRY OLIVIER;
2009
Abstract
The interaction of MMP-12 with its natural substrate elastin has been characterized by NMR spectroscopy (see figure). The catalytic domain of the full-length protein is most affected, with some involvement also of the hemopexin domain. The interaction is largely maintained in the isolated catalytic domain and involves the active site crevice of the protein and 8–11 elastin residues.
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