Fibronectin (FN) is a multifunctional protein serving major roles in the adhesion, migration, differentiation and proliferation of cells with implications in embryonic development, wound healing, and tumorigenesis. The significance of FN in embryonic development has been documented by the embryonic lethality seen in mice when the FN gene is disrupted. FN is a high molecular weight dimeric glycoprotein with disulfide-linked subunits, each with a molecular weight of approximately 220–250 kDa. FN interacts with several other proteins in the ECM including collagen, heparin, fibrin, and cell membrane receptors. The amino acid composition of FN reveals it to be a large modular glycoprotein composed of homologous repeats of three prototypical types of domains known as types-I, II and III. Of these domains, FN type-III (FN-III) repeats are composed of ≈ 90 amino acids making them the largest and most common of the FN subdomains. One of the best characterized interactions between FN and cell membrane receptors is the interaction between the RGD sequence of FN-III domain 10 (FN-10) and the extracellular domain of β1-integrin. This interaction is believed to regulate integrin signaling and therefore may play an important role in integrin-mediated cell differentiation. Here you can see a crystal structure of the human fibronectin type III domain variant, a VEGFR2-specific antagonist (PDB code: 7YPL)

#molecularart ... #immolecular ... #fibronectin ... #antagonist ... #integrin ... #xray

Structure rendered with @proteinimaging and depicted with @corelphotopaint