Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.

Collagen and fibronectin (Fn) are two key extracellular matrix proteins, which are known to interact and jointly shape matrix structure and function. Most proteins that interact with collagen bind only to the native triple-helical form, whereas Fn is unusual in binding strongly to denatured collagen and more weakly to native collagen. The consequences of replacing a Gly by Ser at each position in the required (Gly-Xaa-Yaa) Fn-binding sequence are probed here, using model peptides and a recombinant bacterial collagen system.