Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3.

ABSTRACT: The greater activity of MMP-12 than MMP-3 toward substrates from protein fibrils has been quantified. Why is MMP-12 the more active protease? We looked for behaviors associated with the higher activity of MMP-12 than MMP-3, using nuclear magnetic resonance to monitor backbone dynamics and residue-specific stabilities of their catalytic domain. The proteolytic activities are likely to play important roles in inflammatory diseases of arteries, lungs, joints, and intestines. Nuclear magnetic resonance line broadening indicates that regions surrounding the active sites of both proteases sample conformational substates within milliseconds. The more extensive line broadening in MMP-3 suggests greater sampling of conformational substates, affecting the full length of helix B and beta-strand IV fo

SUBMITTER: Liang X 

PROVIDER: S-EPMC2895380 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature