Abstract
Members of the immunoglobulin superfamily (IgSF) make up the most widely distributed group of cell surface receptors (Barclay et al. 1997). The IgSF comprises proteins containing domains of approximately 100 amino acids folded into a structure (known as the Ig fold) consisting of two antiparallel ß-sheets sandwiched together. Cell adhesion processes involving the Ig-fold are usually mediated by either heterotypic or homotypic protein-protein interactions. The siglec (sialic-acid-binding Ig-like lectins; Crocker et al. 1998) family comprises a group of cell surface molecules, classified by sequence similarity as members of the IgSF, which exhibit functional protein-carbohydrate recognition. The siglecs mediate cellular interactions through the recognition of specific sialylated glycoconjugates as their counter-receptors (Kelm et al. 1994; Freeman et al. 1995; Cornish et al. 1998; Patel et al. 1999; Falco et al. 1999; Nicoll et al. 1999; Angata and Varki 2000a; Floyd et al. 2000; Zhang et al. 2000; Angata and Varki 2000b; Kikly et al. 2000). This group of molecules currently consists of sialoadhesin, CD22, the myelin-associated glycoprotein (MAG), CD33, Siglec-5, Siglec-6, Siglec-7, Siglec-8 and Siglec-9.
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May, A.P., Jones, E.Y. (2001). Sialoadhesin Structure. In: Crocker, P.R. (eds) Mammalian Carbohydrate Recognition Systems. Results and Problems in Cell Differentiation, vol 33. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46410-5_8
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DOI: https://doi.org/10.1007/978-3-540-46410-5_8
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