1G1R

Crystal structure of P-selectin lectin/EGF domains complexed with SLeX

Summary for 1G1R

• Entry DOI: 10.2210/pdb1g1r/pdb
• Related: 1G1Q 1G1S 1G1T
• Descriptor: P-SELECTIN, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: lectin, egf, adhesion molecule, slex, immune system, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P16109
• Total number of polymer chains: 4
• Total formula weight: 79425.92

Authors

Somers, W.S.,Camphausen, R.T. (deposition date: 2000-10-13, release date: 2001-10-13, Last modification date: 2024-10-16)

Primary citation

Somers, W.S.,Tang, J.,Shaw, G.D.,Camphausen, R.T.
Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1.
Cell(Cambridge,Mass.), 103:467-479, 2000

PubMed 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.

PubMed: 11081633
DOI: 10.1016/S0092-8674(00)00138-0

Experimental method

X-RAY DIFFRACTION (3.4 Å)