ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
What it found
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Who cites it
114 citing papers in PubMed, 217 citations in OpenAlex.
- Metadherin: A pivotal oncogene and therapeutic target in head and neck cancer - a systematic review.The Japanese dental science review · 2026Review
- Threonine Phosphorylation Is a Bioreversible Surrogate of Proline Hydroxylation in a Collagen Triple Helix.Journal of the American Chemical Society · 2026Article
- Ligand Design Using Unique Conformations to Preferentially Dock a Specific Site on Collagen-Bound MMP1.Biology · 2026Article
- Drug design using unique conformations to preferentially target a specific site on collagen-bound MMP1.bioRxiv : the preprint server for biology · 2026Article
- Real-time visualization of collagen assembly uncovers metastable properties in hierarchical organization.Nature communications · 2026Article
- Bacterial collagenase harnesses collagen geometry for processive cleavage.Nature communications · 2026Article
- Periodontal ligament stem cells in tissue remodeling: from mechanical forces to inflammatory signals.Stem cell research & therapy · 2025Review
- COL8A1 regulates endothelial phenotype in inflammatory endothelial-to-mesenchymal transition.American journal of physiology. Heart and circulatory physiology · 2025Article
- Endometrial Injury and Its Rescue by Mesenchymal Stem Cells Is Dependent on Estrous Cycle Phase.Journal of cellular and molecular medicine · 2025Article
- Designed Fibril-Forming Mini-Collagens Engineered to Exhibit up to Two Orders of Magnitude Differences in Rates of Matrix Metalloproteinase I Susceptibility.Biomacromolecules · 2025Article
- X-Ray Exposure Induces Structural Changes in Human Breast Proteins.International journal of molecular sciences · 2025Article
- Improved DNA recovery and STR profile development from weathered Bos taurus bones using demineralized bone slices.Journal of forensic sciences · 2025Article
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- Modeling collagen fibril degradation as a function of matrix microarchitecture.bioRxiv : the preprint server for biology · 2024Article
- Novel Insights into the Catalytic Mechanism of Collagenolysis by Zn(II)-Dependent Matrix Metalloproteinase-1.Biochemistry · 2024Article
- Heparan sulfate selectively inhibits the collagenase activity of cathepsin K.Matrix biology : journal of the International Society for Matrix Biology · 2024Article
- A conserved strategy to attack collagen: The activator domain in bacterial collagenases unwinds triple-helical collagen.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Heparan sulfate selectively inhibits the collagenase activity of cathepsin K.bioRxiv : the preprint server for biology · 2024Article
- Mapping the Binding Sites of MMPs on Types II and III Collagens Using Triple-Helical Peptide Toolkits.Methods in molecular biology (Clifton, N.J.) · 2024Article
54 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Collagenases of the matrix metalloproteinase (MMP) family play major roles in morphogenesis, tissue repair, and human diseases, but how they recognize and cleave the collagen triple helix is not fully understood. Here, we report temperature-dependent binding of a catalytically inactive MMP-1 mutant (E200A) to collagen through the cooperative action of its catalytic and hemopexin domains. Contact between the two molecules was mapped by screening the Collagen Toolkit peptide library and by hydrogen/deuterium exchange. The crystal structure of MMP-1(E200A) bound to a triple-helical collagen peptide revealed extensive interactions of the 115-Å-long triple helix with both MMP-1 domains. An exosite in the hemopexin domain, which binds the leucine 10 residues C-terminal to the scissile bond, is critical for collagenolysis and represents a unique target for inhibitor development. The scissile bond is not correctly positioned for hydrolysis in the crystallized complex. A productive binding mode is readily modeled, without altering the MMP-1 structure or the exosite interactions, by axial rotation of the collagen homotrimer. Interdomain flexing of the enzyme and a localized excursion of the collagen chain closest to the active site, facilitated by thermal loosening of the substrate, may lead to the first transition state of collagenolysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.