P-Selectin:EGF Domains


During inflammation, leukocytes tether and roll on the walls of vessels where they are become active. E-, L- and P-selectin proteins are the primary units responsible for the tethering and rolling of these leukocytes.  P-selectin has an N-terminal lectin domain followed by a EGF domain and 9 consensus repeat (CR) domains.  It binds to the P-selectin glycoprotein ligand-1 (PSGL-1), a homodimeric protein of molecular weight 240K, expressed on leukocytes, in part through the sialyl-Lewisx (SLEX) CHO on the ligand.  The interaction between P-selectin and PSGL-1 mediates the "rolling" binding event.  The following is a series of images of the crystalline structure of the lectin:EGF domain complexed to SLEX.

Wire Frame


Backbone and sidechains

Backbone, sidechains, and CHO

Cartoon and Wireframe

Cartoon, Wireframe, and CHO

Chain B and CHO

with Sia (red), Gal (orange), 1NA (yellow), and Fuc (green)

Dot surface and Wireframe