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

@article{Sako1995ASP,
  title={A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding},
  author={D. Sako and K. Comess and K. Barone and R. Camphausen and D. Cumming and G. Shaw},
  journal={Cell},
  year={1995},
  volume={83},
  pages={323-331}
}
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… Expand
Structure and function of the selectin ligand PSGL-1.
  • R. Cummings
  • Chemistry, Medicine
  • Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas
  • 1999
Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin.
Binding of Glycosulfopeptides to P-selectin Requires Stereospecific Contributions of Individual Tyrosine Sulfate and Sugar Residues*
  • A. Leppänen, Steven P. White, Jari Helin, Rodger P. McEver, R. Cummings
  • Medicine, Chemistry
  • The Journal of Biological Chemistry
  • 2000
A Novel Glycosulfopeptide Binds to P-selectin and Inhibits Leukocyte Adhesion to P-selectin*
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