Sandbox Q123

spinqualitylabelsall models Human glycosylated fibronectin gelatin-binding domain complex with PEG400, dodecaethylene glycol and Zn+2 ions (grey) (PDB code 3m7p) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural insights Fibronectin (FN) is a dimer of homologous monomers linked by S-S bond. Each monomer contains 3 types of repeating units: FN I, FN II and FN III. Type I and type II repeats are disulfide-bonded loops, containing about 45 and 60 amino-acids each, while type III repeats are about 90 amino-acids long without S-S bonds. Each module contains several numbered protein binding domains, i.e., FN I6-FN II1-2-FN I7-9 is the gelatin binding domain (GBD). Function FN is a glycoprotein which binds extracellular matrix components like integrin, collagen, fibrin and others. It plays an important role in cell adhesion, migration and differentiation . In addition, FN is also important for the adherence of pathogens to host tissues and the linking between proteins and cells. Relevance FN is associated with inflammation area and the process of wound healing. Local treatment of fibronectin has a potential role in accelerating wound closure and the decrease in fibronectin expression can result in poorly healed wound. In addition, Fn is considered as a potential marker for radiation resistance. Disease FN can be divided into soluble and insoluble forms. Soluble FN can be found in plasma and other fluids which circulate in human body. The insoluble form is mainly found on the surface of cells and the extracellular matrix (ECM). Although FN can be synthesised by many cell types, soluble (plasma) FN was found to be mainly produced by hepatocytes. Therefore, for patients with liver diseases, the concentration of their plasma FN is lower. In addition, Overexpression of Fn1 is associated with lung cancer. 3D Structures of Fibronectin Fibronectin 3D structures