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Cell
Volume 83, Issue 2, 20 October 1995, Pages 323-331
 
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doi:10.1016/0092-8674(95)90173-6    
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Copyright © 1995

Article

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

Dianne Sako *, Kenneth M. Comess *, Karen M. Barone , Raymond T. Camphausen , Dale A. Cumming and Gray D. Shaw

Genetics Institute Small Molecule Drug Discovery Group 85 Bolton Street, Cambridge, Massachusetts 02140, USA


Received 23 May 1995; 
Revised 27 September 1995. 
Available online 14 April 2004.

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 0-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 0-linked glycans, constitutes the high affinity P-selectin-binding site.

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* These authors contributed equally to this work.


Cell
Volume 83, Issue 2, 20 October 1995, Pages 323-331
 
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