Abstract
Fibronectin is a large (~440 kDa) dimeric glycoprotein found in body fluids and the extracellular matrix of higher animals. This protein has been shown to affect numerous biological processes. Most of the biological functions of fibronectin appear to be related to its ability to serve as a substrate for the adhesion of eukaryotic cells (for review, see Hynes, 1985; Yamada, 1983). The cellular receptors that mediate cell adhesion to fibronectin are of the integrin type, a family of heterodimeric receptors consisting of an α-chain and a β-chain. Several integrins recognize structures in the fibronectin molecule. Thus, α5β1 and αvβ3 recognize and bind to a Arg-Gly-Asp (RGD) sequence located in the central part of fibronectin (Hynes, 1992).
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Gurusiddappa, S., Höök, M. (1994). Synthetic Peptides Mimic the Active Sites of Fibronectin Receptors from Gram-Positive Bacteria. In: Basava, C., Anantharamaiah, G.M. (eds) Peptides. Birkhäuser Boston. https://doi.org/10.1007/978-1-4615-8176-5_16
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DOI: https://doi.org/10.1007/978-1-4615-8176-5_16
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