A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding.
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Sako D, Comess KM, Barone KM, Camphausen RT, Cumming DA, Shaw GD
A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding.
Cell. 1995 Oct 20;83(2):323-31.
- PubMed ID
- 7585949 [ View in PubMed]
- Abstract
P-selectin glycoprotein ligand 1 (PSGL-1) is a mucin-like glycoprotein expressed on the surface of myeloid cells and serves as the high affinity counterreceptor for P-selectin. The PSGL-1-P-selectin interaction is calcium dependent and requires presentation of sialyl-Lewisx (sLex)-type structures on the O-linked glycans of PSGL-1. We report here the identification of a non-carbohydrate component of the binding determinant that is critical for high affinity binding to P-selectin. Located within the first 19 amino acids, this anionic polypeptide segment contains at least one sulfated tyrosine residue. We propose that this sulfotyrosine-containing segment of PSGL-1, in conjunction with sLex presented on O-linked glycans, constitutes the high affinity P-selectin-binding site.