Crystal Structure of an Active Form of Human MMP-1
2006
Structure of Active Human MMP-1
publication
Evidence: high
Author Information
Author(s): Shalini Iyer, Robert Visse, Hideaki Nagase, K. Ravi Acharya
Primary Institution: University of Bath and Imperial College London
Hypothesis
The study aims to elucidate the crystal structure of the active form of human MMP-1 to understand its role in collagen degradation.
Conclusion
The crystal structure reveals significant differences between the pro and active forms of MMP-1, providing insights into its catalytic mechanism.
Supporting Evidence
- The structure was determined at a resolution of 2.67 Å.
- This is the first MMP-1 structure that is free of inhibitor.
- A water molecule essential for peptide hydrolysis was observed at the active site.
Takeaway
Scientists looked at the shape of a protein called MMP-1, which helps break down collagen in our bodies, to understand how it works better.
Methodology
The study used X-ray crystallography to determine the structure of the active form of MMP-1.
Digital Object Identifier (DOI)
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