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Fig. 1. (A) Structural diagrams representing P-, E- and L-selectin. The selectins are rigid, asymmetric molecules that share structural similarities including the presence of the C-type lectin domain, followed by an epidermal-growth-factor-like (EGF) motif, a variable series of short consensus repeats (nine, six and two for P-, E- and L-selectins, respectively), a transmembrane domain (TM) and a cytoplasmic tail (cyto). There is also a high degree of homology between the three proteins within each region. (B) Selectin-mediated leukocyte recruitment. PSGL-1 on free-flowing leukocytes tethers to E- and/or P-selectin on activated endothelial cells, allowing leukocytes to roll to sites of infection or inflammation. E-Selectin might also bind to an as-yet-unidentified leukocyte glycosphingolipid. PSGL-1 on adherent leukocytes participates in secondary tethering by interacting with L-selectin on free-flowing leukocytes.





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