PMID: 11081633

 

    Legend: Gene, Sites

Title : 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

Abstract :

1. 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
2. The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors , including PSGL-1
3. Here, we report crystal structures of human P- and E-selectin constructs containing the lectin and EGF ( LE ) domains co-complexed with SLe(X)
4. 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)
5. 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

Output (sent_index, trigger, protein, sugar, site):

• 2. glycoprotein, , glycoprotein, -, -

Output(Part-Of) (sent_index, protein, site):

• 3. EGF, domains
• 4. PSGL-1, domain

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
E-selectin	6401	0
P- and E-selectin	6403	3
P-, E- and L-selectin	6402	1
P-selectin	6403	5
structure of P-selectin LE	6403	4