Introduction
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
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
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