Insights into the Molecular Basis of Leukocyte Tethering and Rolling Revealed by Structures of P- and E-Selectin Bound to SLe super(x) and PSGL-1

P-, E- and L-selectin constitute a family of cell adhesion receptors that mediate the initial tethering and rolling of leukocytes on inflamed endothelium as a prelude to their firm attachment and extravasation into tissues. The selectins bind weakly to sialyl Lewis super(x) (SLe super(x))-like glyca...

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Bibliographic Details
Published in:Cell 2000-10, Vol.103 (3), p.467-479
Main Authors: Somers, W S, Tang, Jin, Shaw, G D, Camphausen, R T
Format: Article
Language:English
Subjects:
E-selectin
epidermal growth factor
P-selectin
sialyl Lewis x antigen
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Summary:P-, E- and L-selectin constitute a family of cell adhesion receptors that mediate the initial tethering and rolling of leukocytes on inflamed endothelium as a prelude to their firm attachment and extravasation into tissues. The selectins bind weakly to sialyl Lewis super(x) (SLe super(x))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1. Here, we report crystal structures of human P- and E-selectin constructs containing the lectin and EGF (LE) domains co-complexed with SLe super(x). We also present the crystal structure of P-selectin LE co-complexed with the N-terminal domain of human PSGL-1 modified by both tyrosine sulfation and SLe super(x). These structures reveal differences in how E- and P-selectin bind SLe super(x) and the molecular basis of the high-affinity interaction between P-selectin and PSGL-1.
ISSN:0092-8674