PSGL - 1

P-selectin glycoprotein ligand-1 is a 240 kDa homodimer consisting of two 120kDa polypeptide chains. PSGL-1 is constitutively expressed on all leukocytes. PSGL-1 is primarily found on the tips of the microvilli. PSGL-1 can bind to P-selectin on the endothelium when decorated with appropriate sugars. The structure of functional PSGL-1 includes the sialyl-Lewisx component. The PSGL-1 gene encodes a transmembrane polypeptide rich in proline, serine and threonine residues typical of mucin-type glycoproteins. The O-linked glycans displayed by PSGL-1 must undergo two specific post-translational modifications in order for it to function as a counter-receptor for P-selectin: a(1,3) fucosylation and a(2,3) sialylation. Bonds between P-selectin and PSGL-1 primarily mediate the rolling phase of the adhesion cascade.

View various information about this molecule at the National Center for Biotechnology Information.


Search similar protein and nucleotide sequences between various species using BLAST (Basic Local Alignment Search Tool)
  • Copy the desired sequence from the GenBank Database and paste it into the text box on the BLAST page.
  • Search results will provide a list of homologous molecules and show a statistical relationship between high-scoring segment pairs.
  • For more information on the results, consult the BLAST Help Manual.


Read the following categorized abstracts or link to Medline to conduct your own query.

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