1G1S: P-selectin Lectin/egf Domains Complexed With Psgl-1 Peptide

Citation:
Abstract
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 Lewisx (SLe(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(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(X). These structures reveal differences in how E- and P-selectin bind SLe(X) and the molecular basis of the high-affinity interaction between P-selectin and PSGL-1.
PDB ID: 1G1SDownload
MMDB ID: 17784
PDB Deposition Date: 2000/10/13
Updated in MMDB: 2001/11
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1G1S: tetrameric; determined by author
Molecular Components in 1G1S
Label Count Molecule
Proteins (4 molecules)
2
P-selectin(Gene symbol: SELP)
Molecule annotation
2
Psgl-1 Peptide(Gene symbol: SELPLG)
Molecule annotation
Chemicals (23 molecules)
1
2
2
7
3
2
4
2
5
4
6
2
7
2
8
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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