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Despite its biological importance, the interaction between fibronectin (FN) and collagen, two abundant and crucial tissue components, has not been well characterized on a structural level. Here, we analyzed the four interactions formed between epitopes of collagen type I and the collagen-binding fragment (gelatin-binding domain (GBD)) of human FN using solution NMR, fluorescence, and small angle x-ray scattering methods. Collagen association with FN modules (8-9)FnI occurs through a conserved structural mechanism but exhibits a 400-fold disparity in affinity between collagen sites. This disparity is reduced in the full-length GBD, as (6)FnI(1-2)FnII(7)FnI binds a specific collagen epitope next to the weakest (8-9)FnI-binding site. The cooperative engagement of all GBD modules with collagen results in four broadly equipotent FN-collagen interaction sites. Collagen association stabilizes a distinct monomeric GBD conformation in solution, giving further evidence to the view that FN fragments form well defined functional and structural units.

Original publication




Journal article


J Biol Chem

Publication Date





17441 - 17450


Collagen, Extracellular Matrix Proteins, Fibronectin, GBD, NMR, SAXS, X-ray Crystallography, Amino Acid Sequence, Collagen Type I, Fibronectins, Humans, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Interaction Domains and Motifs, Protein Stability, Protein Structure, Quaternary, Protein Structure, Secondary, Solutions, Tomography, X-Ray Computed