Abstract:
:Matrix 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.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Singh W,Fields GB,Christov CZ,Karabencheva-Christova TGdoi
10.3390/ijms17101727subject
Has Abstractpub_date
2016-10-14 00:00:00issue
10issn
1422-0067pii
ijms17101727journal_volume
17pub_type
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