262283-34-1Relevant articles and documents
Tyrosine sulfation on a PSGL-1 glycopeptide influences the reactivity of glycosyltransferases responsible for synthesis of the attached O-glycan [16]
Koeller, Kathryn M.,Smith, Mark E. B.,Wong, Chi-Huey
, p. 742 - 743 (2007/10/03)
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Chemoenzymatic synthesis of PSGL-1 glycopeptides: Sulfation on tyrosine affects glycosyltransferase-catalyzed synthesis of the O-glycan
Koeller, Kathryn M.,Smith, Mark E. B.,Wong, Chi-Huey
, p. 1017 - 1025 (2007/10/03)
PSGL-1 is the primary glycoprotein ligand for P-selectin during the inflammatory response. Interestingly, the N-terminal sequence, containing both a site of tyrosine sulfation and an O-glycan, has been shown to bind to P-selectin with an affinity similar to full-length PSGL-1. To further characterize this system, the synthesis of glycopeptides from PSGL-1 was undertaken. The synthesis involved both solution- and solid-phase synthesis, as well as enzymatic transformations. During the synthesis, notable reactivity differences of the glycosyltransferases toward sulfated and unsulfated versions of the same glycopeptides were observed. (C) 2000 Elsevier Science Ltd.