ArticleProceedings of the National Academy of Sciences of the United States of America2012
Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition.
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 88 papers.
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Who cites it
88 citing papers in PubMed, 178 citations in OpenAlex.
- HSP47 in Mitochondria: Roles in Apoptosis, Signal Transduction, and Protein and Virus Transportation.Cells · 2026Review
- Procollagen 1 assembles into phase-separated condensates in the endoplasmic reticulum.The Journal of cell biology · 2026Article
- Proteomic Profiling Reveals Region-Specific Brain Responses During Acclimation to Elevated Water Temperature in Atlantic Salmon (Proteomes · 2026Article
- Heat Shock Protein 47 as a Novel Predictive and Diagnostic Biomarker for Thrombosis in Hepatocellular Carcinoma.Journal of hepatocellular carcinoma · 2026Article
- Ai-Assisted Discovery of a Direct Physical Interaction Between a Venom Serpin from the Parasitoid WaspToxins · 2025Article
- The Role of HSP47 in Thrombotic Disorders: Molecular Mechanism and Therapeutic Potential.Current issues in molecular biology · 2025Review
- Deciphering the folding code of collagens.Nature communications · 2025Article
- The administration of exogenous HSP47 as a collagen-specific therapeutic approach.JCI insight · 2025Article
- Treatment with a superoxide dismutase mimetic for joint preservation during 35 and 75 days in orbit aboard the international space station, and after 120 days recovery on Earth.Life sciences in space research · 2025Article
- Identification of gene signatures and potential pharmaceutical candidates linked to COVID-19-related depression based on gene expression profiles.Frontiers in pharmacology · 2025Article
- Application of Tendon-Derived Matrix and Carbodiimide Crosslinking Matures the Engineered Tendon-Like Proteome on Meltblown Scaffolds.Journal of tissue engineering and regenerative medicine · 2025Article
- Pleiotropic effects of a recessive Col1a2 mutation occurring in a mouse model of severe osteogenesis imperfecta.PloS one · 2025Article
- O-GlcNAcylated Hsp47 as a predictive biomarker in colorectal cancer: Kaempferol targets OGT-collagen axis for therapeutic intervention.International journal of biological sciences · 2025Article
- Improving the diffraction quality of heat-shock protein 47 crystals.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Molecular basis of urostyle development in frogs: genes and gene regulation underlying an evolutionary novelty.Open biology · 2024Article
- Identification of tumor stemness and immunity related prognostic factors and sensitive drugs in head and neck squamous cell carcinoma.Scientific reports · 2024Article
- Article
- Insights into the Mechanism of Action of the Degraded Limonoid Prieurianin.International journal of molecular sciences · 2024Review
- A model for collagen secretion by intercompartmental continuities.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Regulation of epidermal barrier function and pathogenesis of psoriasis by serine protease inhibitors.Frontiers in immunology · 2024Review
28 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen is the most abundant protein in animals and is a major component of the extracellular matrix in tissues such as skin and bone. A distinctive structural feature of all collagen types is a unique triple-helical structure formed by tandem repeats of the consensus sequence Xaa-Yaa-Gly, in which Xaa and Yaa frequently are proline and hydroxyproline, respectively. Hsp47/SERPINH1 is a procollagen-specific molecular chaperone that, unlike other chaperones, specifically recognizes the folded conformation of its client. Reduced functional levels of Hsp47 were reported in severe recessive forms of osteogenesis imperfecta, and homozygous knockout is lethal in mice. Here we present crystal structures of Hsp47 in its free form and in complex with homotrimeric synthetic collagen model peptides, each comprising one Hsp47-binding site represented by an arginine at the Yaa-position of a Xaa-Yaa-Gly triplet. Two of these three binding sites in the triple helix are occupied by Hsp47 molecules, which bind in a head-to-head fashion, thus making extensive contacts with the leading and trailing strands of the collagen triple helix. The important arginine residue within the Xaa-Arg-Gly triplet is recognized by a conserved aspartic acid. The structures explain the stabilization of the triple helix as well as the inhibition of collagen-bundle formation by Hsp47. In addition, we propose a pH-dependent substrate release mechanism based on a cluster of histidine residues.
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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.