Selectins represent a family of three structurally and functionally related adhesion molecules: E-selectin, P-selectin and L-selectin. Each selectin consists of an extracellular lectin-like domain, an EGF-like domain, and variable numbers of a consensus repeat bearing homology to complement proteins, followed by transmembrane and short intracellular sequences. The lectin-like domains are primarily responsible for Ca2+-dependent interactions with fucosylated, mucin-like ligands. Functionally, the rapid association and dissociation rate constants that characterize selectin-mediated adhesion allow selectins to function as important initiators of leukocyte adhesion to endothelium under conditions of shear flow. A role for selectins as signal transducing receptors is also now becoming evident.

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