ArticleProceedings of the National Academy of Sciences of the United States of America2008
Structural basis of sequence-specific collagen recognition by SPARC.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 134 citations in OpenAlex.
- Triple-helical ligands for collagen-binding proteins improve cartilage extracellular matrix production in nasal chondrocytes.Materials today. Bio · 2026Article
- Variant-specific RNA testing resolves variants of uncertain significance in exome testing.BMC genomics · 2026Article
- Impact of Stiffness and Cell-Binding Motif Availability on the Cell-Specific Response to Collagen-Based Macromolecular Materials.Biomacromolecules · 2026Article
- Integrative bioinformatic analysis identifies an extracellular matrix gene signature linked to muscle adaptation to endurance and resistance training.Physiological reports · 2026Article
- Hydrogels Formed by the Self-Assembly of Collagen-Mimetic Peptides With a Constrained Backbone Structure.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Triple Helical-Peptides: Collagen-Mimicking Tools for Tissue Engineering.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Molecular drivers of osteogenesis imperfecta: a cellular and extracellular collagen disease.Clinical science (London, England : 1979) · 2025Review
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- β-Turn Mimicking Crosslinking Provides Hyperstability and Fast Folding Kinetics for Short Collagen Triple Helices.Chembiochem : a European journal of chemical biology · 2025Article
- Therapeutic Potential of Exercise-Induced SPARC in Bone Health?Biomedicines · 2025Article
- Deciphering the folding code of collagens.Nature communications · 2025Article
- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- Non-invasive in vivo imaging of changes in Collagen III turnover in myocardial fibrosis.Npj imaging · 2024Article
- Synthetic peptides activating discoidin domain receptor 2 and collagen-binding integrins cooperate to stimulate osteoblast differentiation of skeletal progenitor cells.Acta biomaterialia · 2023Article
- Cell Competition Shapes Metastatic Latency and Relapse.Cancer discovery · 2023Article
- Serum CRP interacts with SPARC and regulate immune response in severe cases of COVID-19 infection.Frontiers in immunology · 2023Article
- Discoidin domain receptors; an ancient family of collagen receptors has major roles in bone development, regeneration and metabolism.Frontiers in dental medicine · 2023Article
- Collagen-Specific Molecular Magnetic Resonance Imaging of Prostate Cancer.International journal of molecular sciences · 2022Article
- Loss of core-fucosylation of SPARC impairs collagen binding and contributes to COPD.Cellular and molecular life sciences : CMLS · 2022Article
- Effect of Cold Atmospheric Plasma (CAP) on Osteogenic Differentiation Potential of Human Osteoblasts.International journal of molecular sciences · 2022Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
Protein interactions with the collagen triple helix play a critical role in collagen fibril formation, cell adhesion, and signaling. However, structural insight into sequence-specific collagen recognition is limited to an integrin-peptide complex. A GVMGFO motif in fibrillar collagens (O denotes 4-hydroxyproline) binds 3 unrelated proteins: von Willebrand factor (VWF), discoidin domain receptor 2 (DDR2), and the extracellular matrix protein SPARC/osteonectin/BM-40. We report the crystal structure at 3.2 A resolution of human SPARC bound to a triple-helical 33-residue peptide harboring the promiscuous GVMGFO motif. SPARC recognizes the GVMGFO motifs of the middle and trailing collagen chains, burying a total of 720 A(2) of solvent-accessible collagen surface. SPARC binding does not distort the canonical triple helix of the collagen peptide. In contrast, a critical loop in SPARC is substantially remodelled upon collagen binding, creating a deep pocket that accommodates the phenylalanine residue of the trailing collagen chain ("Phe pocket"). This highly restrictive specificity pocket is shared with the collagen-binding integrin I-domains but differs strikingly from the shallow collagen-binding grooves of the platelet receptor glycoprotein VI and microbial adhesins. We speculate that binding of the GVMGFO motif to VWF and DDR2 also results in structural changes and the formation of a Phe pocket.
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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.