ArticleThe Journal of biological chemistry2014
The cysteine-rich region of type VII collagen is a cystine knot with a new topology.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Dynamic Self-Clickable Decellularized Matrix Hydrogels for Regulating Vascularity and Enhancing Muscle Regeneration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The Fate of Intranasally Instilled Silver Nanoarchitectures.Nano letters · 2022Article
- The Immunogenetics of Autoimmune Blistering Diseases.Advances in experimental medicine and biology · 2022Review
- Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites.FEBS open bio · 2020Article
- Reversible Covalent End-Capping of Collagen Model Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Optimal interstrand bridges for collagen-like biomaterials.Journal of the American Chemical Society · 2014Article
- Intrinsically disordered proteins and biomineralization.Matrix biology : journal of the International Society for Matrix BiologyReview
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3 authors.
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Abstract
Collagens are a group of extracellular matrix proteins with essential functions for skin integrity. Anchoring fibrils are made of type VII collagen (Col7) and link different skin layers together: the basal lamina and the underlying connective tissue. Col7 has a central collagenous domain and two noncollagenous domains located at the N and C terminus (NC1 and NC2), respectively. A cysteine-rich region of hitherto unknown function is located at the transition of the NC1 domain to the collagenous domain. A synthetic model peptide of this region was investigated by CD and NMR spectroscopy. The peptide folds into a collagen triple helix, and the cysteine residues form disulfide bridges between the different strands. The eight cystine knot topologies that are characterized by exclusively intermolecular disulfide bridges have been analyzed by molecular modeling. Two cystine knots are energetically preferred; however, all eight disulfide bridge arrangements are essentially possible. This novel cystine knot is present in type IX collagen, too. The conserved motif of the cystine knot is CX3CP. The cystine knot is N-terminal to the collagen triple helix in both collagens and therefore probably impedes unfolding of the collagen triple helix from the N terminus.
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