Fig. 1

Diagram of FN1 structure and its splice variants. a) FN1 monomer is composed by type I, type II and type III modules (FN I-III). The type III EDA (a) and EDB (b) repeats and the variable region V are alternatively spliced. The binding repeats for cellular surface integrin receptors and for other proteins, such as FN1, heparin, fibrin, collagen, fibrillin, tenascin, TGFβ, syndecan 4 and fibulin, are reported. The modules are grouped into functional domains: N-terminal 70-kDa domain (FNI1–9), the 120-kDa central binding domain (FNIII1–12) and the heparin-binding domain HEPII (FNIII12–14). The two cysteine residues at the C-terminus possess the thiol functional groups to build disulfide bonds with another FN1 monomer forming the FN1 dimeric protein. b) Schematic representation of FN1 alternative splicing variants. Created with BioRender.com