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    Cell. 1995 Oct 20;83(2):323-31.

    A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding.

    Sako D, Comess KM, Barone KM, Camphausen RT, Cumming DA, Shaw GD.

    Genetics Institute, Small Molecule Drug Discovery Group, Cambridge, Massachusetts 02140, USA.

    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.

    PMID: 7585949 [PubMed - indexed for MEDLINE]

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