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. doi: 10.1016/0092-8674(95)90173-6.


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.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • DNA Mutational Analysis
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Neuraminidase / metabolism
  • P-Selectin / metabolism*
  • Peptides / chemistry*
  • Protein Binding
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Sequence Deletion
  • Structure-Activity Relationship
  • Tyrosine / analogs & derivatives*
  • Tyrosine / analysis


  • Membrane Glycoproteins
  • P-Selectin
  • P-selectin ligand protein
  • Peptides
  • Recombinant Fusion Proteins
  • tyrosine O-sulfate
  • Tyrosine
  • Neuraminidase