1g1t

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Revision as of 13:30, 20 November 2007

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spinqualitylabelsall models 1g1t, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF E-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH SLEX

Overview

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.

About this Structure

1G1T is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.

Reference

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., Somers WS, Tang J, Shaw GD, Camphausen RT, Cell. 2000 Oct 27;103(3):467-79. PMID:11081633

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