Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin.
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Alon R, Bayer EA, Wilchek M
Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin.
Biochem Biophys Res Commun. 1990 Aug 16;170(3):1236-41.
- PubMed ID
- 2390089 [ View in PubMed]
- Abstract
Streptavidin binds at low levels and high affinity to cell surfaces, the cause of which can be traced to the occurrence of a sequence containing RYD (Arg-Tyr-Asp) in the protein molecule. This binding is enhanced in the presence of biotin. Cell-bound streptavidin can be displaced by fibronectin, as well as by RGD- and RYD-containing peptides. In addition, streptavidin can displace fibronectin from cell surfaces. The RYD sequence of streptavidin thus mimics RGD (Arg-Gly-Asp), the universal recognition domain present in fibronectin and other adhesion-related molecules. The observed adhesion to cells has no relevance to biotin-binding since the RYD sequence is not part of the biotin-binding site of streptavidin. Since the use of streptavidin in avidin-biotin technology is based on its biotin-binding properties, researchers are hereby warned against its indiscriminate use in histochemical and cytochemical studies.