期刊
RSC ADVANCES
卷 6, 期 28, 页码 23223-23232出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c6ra03033e
关键词
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资金
- Marie Curie International Career Development Fellowships
- NSCCS grants
- HEC-Biosim grants
- Northumbria University
- NIH [CA098799]
Collagenolysis is catalyzed by enzymes from the matrix metalloproteinase (MMP) family, where one of the most studied is MMP-1. The X-ray crystallographic structure of MMP-1 complexed with a collagen-model triple-helical peptide (THP) provided important atomistic information, but few details on the effects of the conformational flexibility on catalysis. In addition, the role of the linker region between the catalytic (CAT) and hemopexin-like (HPX) domains was not defined. In order to reveal the dynamics and correlations of MMP-1 comprehensive atomistic molecular dynamics simulations of an MMP-1$ THP complex was performed. To examine the role of the linker region for MMP-1 function simulations with linker regions from MT1-MMP/ MMP-14 and MMP-13 replacing the MMP-1 linker region were performed. The MD studies were in good agreement with the experimental observation that in the MMP-1$ THP X-ray crystallographic structure MMP-1 is in a closed conformation. MD revealed that the interactions of the THP with the both the CAT and HPX domains of MMP-1 are dynamic in nature, and the linker region of MMP-1 influences the interactions and dynamics of both the CAT and HPX domains and collagen binding to MMP-1.
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