Effects of Mutations on Structure–Function Relationships of Matrix Metalloproteinase-1
AbstractMatrix metalloproteinase-1 (MMP-1) is one of the most widely studied enzymes involved in collagen degradation. Mutations of specific residues in the MMP-1 hemopexin-like (HPX) domain have been shown to modulate activity of the MMP-1 catalytic (CAT) domain. In order to reveal the structural and conformational effects of such mutations, a molecular dynamics (MD) study was performed of in silico mutated residues in the X-ray crystallographic structure of MMP-1 complexed with a collagen-model triple-helical peptide (THP). The results indicate an important role of the mutated residues in MMP-1 interactions with the THP and communication between the CAT and the HPX domains. Each mutation has a distinct impact on the correlated motions in the MMP-1•THP. An increased collagenase activity corresponded to the appearance of a unique anti-correlated motion and decreased correlated motions, while decreased collagenase activity corresponded both to increased and decreased anti-correlated motions. View Full-Text
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Singh, W.; Fields, G.B.; Christov, C.Z.; Karabencheva-Christova, T.G. Effects of Mutations on Structure–Function Relationships of Matrix Metalloproteinase-1. Int. J. Mol. Sci. 2016, 17, 1727.
Singh W, Fields GB, Christov CZ, Karabencheva-Christova TG. Effects of Mutations on Structure–Function Relationships of Matrix Metalloproteinase-1. International Journal of Molecular Sciences. 2016; 17(10):1727.Chicago/Turabian Style
Singh, Warispreet; Fields, Gregg B.; Christov, Christo Z.; Karabencheva-Christova, Tatyana G. 2016. "Effects of Mutations on Structure–Function Relationships of Matrix Metalloproteinase-1." Int. J. Mol. Sci. 17, no. 10: 1727.
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