ArticleThe Journal of biological chemistry2010
The NC2 domain of collagen IX provides chain selection and heterotrimerization.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Around the collagen triple helix: an introduction to studying associated genetic and acquired diseases.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- The staphylococcal collagen adhesin CNA35 effectively detects collagen and its fragments in blots after SDS-PAGE.Matrix biology plus · 2025Article
- Deciphering the folding code of collagens.Nature communications · 2025Article
- An Ancient MHC-Linked Gene Encodes a Nonrearranging Shark Antibody, UrIg, Convergent with IgG.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- A recombinant technique for mapping functional sites of heterotrimeric collagen helices: Collagen IV CB3 fragment as a prototype for integrin binding.The Journal of biological chemistry · 2023Article
- An epitope-enriched immunogen expands responses to a conserved viral site.Cell reports · 2022Article
- Collagen Mimetic Peptides.Bioengineering (Basel, Switzerland) · 2021Review
- Type XIX collagen: a promising biomarker from the basement membranes.Neural regeneration research · 2020Review
- Structural insight for chain selection and stagger control in collagen.Scientific reports · 2016Article
- Article
- Vascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding.The Journal of biological chemistry · 2013Article
- The NC2 domain of type IX collagen determines the chain register of the triple helix.The Journal of biological chemistry · 2012Article
- Crystal structure of the human collagen XV trimerization domain: a potent trimerizing unit common to multiplexin collagens.Matrix biology : journal of the International Society for Matrix Biology · 2011Article
- The collagen family.Cold Spring Harbor perspectives in biology · 2011Review
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Authors and funding
6 authors.
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Abstract
The mechanism of chain selection and trimerization of fibril-associated collagens with interrupted triple helices (FACITs) differs from that of fibrillar collagens that have special C-propeptides. We recently showed that the second carboxyl-terminal non-collagenous domain (NC2) of homotrimeric collagen XIX forms a stable trimer and substantially stabilizes a collagen triple helix attached to either end. We then hypothesized a general trimerizing role for the NC2 domain in other FACITs. Here we analyzed the NC2 domain of human heterotrimeric collagen IX, the only member of FACITs with all three chains encoded by distinct genes. Upon oxidative folding of equimolar amounts of the alpha1, alpha2, and alpha3 chains of NC2, a stable heterotrimer with a disulfide bridge between alpha1 and alpha3 chains is formed. Our experiments show that this heterotrimerization domain can stabilize a short triple helix attached at the carboxyl-terminal end and allows for the proper oxidation of the cystine knot of type III collagen after the short triple helix.
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