Implications for Collagen Binding from the Crystallographic Structure of Fibronectin 6FnI1–2FnII7FnI

摘要: Collagen and fibronectin (FN) are two abundant essential components of the vertebrate extracellular matrix; they interact directly with cellular receptors affect cell adhesion migration. Past studies identified a FN fragment comprising six modules, 6FnI1–2FnII7–9FnI, termed gelatin binding domain (GBD) as responsible for collagen interaction. Recently, we showed that GBD binds tightly to specific site within type I determined structure domains 8–9FnI in complex peptide from site. Here, present crystallographic 6FnI1–2FnII7FnI, which form compact, globular unit through interdomain interactions. Analysis NMR titrations single-stranded peptides reveals dominant interaction surface on 2FnII 7FnI; similar appears involved interactions triple-helical peptides. Models complete GBD, based new 8–9FnI·collagen show continuous putative surface. We explore implications this model using long discuss our findings context fibrils.