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. Author manuscript; available in PMC: 2010 Apr 15.
Published in final edited form as: J Cell Biochem. 2009 Apr 15;106(6):957–966. doi: 10.1002/jcb.22076

1). Structural motifs of SED1/MFG-E8 and Del1.

1)

Both proteins contain Notch like-EGF repeats, the second of which possess an RGD integrin-binding motif, as well as two discoidin/F5/8 C domains that are able to bind phospholipid bilayers and/or extracellular glycosides via 2-3 hairpin loops projecting from the central barrel core. SED1/MFG-E8 and Del1 are believed to facilitate cell-matrix adhesion via RGD-dependent binding to cell surface αvβ3/5 integrin receptors, whereas the discoidin/F5/8C domain is also thought to bind to cell membranes via intercalation into the lipid bilayer. Alternatively, the discoidin/F5/8C domains may coordinate binding to extracellular glycoside substrates, similar to that seen in the sugar-binding discoidin domains. Del1 contains a third EGF repeat not found within SED1.

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