ArticleProtein science : a publication of the Protein Society2003
Mapping Hsp47 binding site(s) using CNBr peptides derived from type I and type II collagen.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 29 citations in OpenAlex.
- Exogenous supply of Hsp47 triggers fibrillar collagen deposition in skin cell cultures in vitro.BMC molecular and cell biology · 2020Article
- Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Direct in vitro and in vivo evidence for interaction between Hsp47 protein and collagen triple helix.The Journal of biological chemistry · 2012Article
- Translationally controlled tumor protein is a novel heat shock protein with chaperone-like activity.Biochemical and biophysical research communications · 2009Article
- A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta.PLoS genetics · 2009Article
- Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.PloS one · 2007Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
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Abstract
As a crucial molecular chaperone in collagen biosynthesis, Hsp47 interacts with the nascent form as well as the mature triple-helical form of procollagen. The location(s) of Hsp47 binding sites on the collagen molecule are, as yet, unknown. We have examined the substrate specificity of Hsp47 in vitro using well-characterized CNBr peptide fragments of type I and type II collagen along with radiolabeled, recombinant Hsp47. Interaction of these peptides with Hsp47 bound to collagen-coated microtiter wells showed several binding sites for Hsp47 along the length of the alpha1 and alpha2 chains of type I collagen and the alpha1 chain of type II collagen, with the N-terminal regions showing the strongest affinities. The latter observation was also supported by the results of a ligand-blot assay. Except for two peptides in the alpha2(I) chain, peptides that showed substantial binding to Hsp47 did so in their triple-helical and not random-coil form. Unlike earlier studies that used peptide models for collagen, the results obtained here on fragments of type I and type II collagen identify, for the first time, binding of Hsp47 to specific regions of the collagen molecule. They also point to additional structural requirements for Hsp47 binding besides the known preference for third-position Arg residues and the triple-helical conformation.
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