Title : The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation.

Pub. Date : 2007 Apr

PMID : 17215257






3 Functional Relationships(s)
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1 We have previously shown that the lectin domain of GalNAc-T4 modulates its substrate specificity to enable unique GalNAc-glycopeptide specificities and that this effect is selectively inhibitable by GalNAc; however, direct evidence of carbohydrate binding of GalNAc-transferase lectins has not been previously presented. N-acetylgalactosaminuronic acid polypeptide N-acetylgalactosaminyltransferase 4 Homo sapiens
2 Here, we report the direct carbohydrate binding of two GalNAc-transferase lectin domains, GalNAc-T4 and GalNAc-T2, representing isoforms reported to have distinct glycopeptide activity (GalNAc-T4) and isoforms without apparent distinct GalNAc-glycopeptide specificity (GalNAc-T2). N-acetylgalactosaminuronic acid polypeptide N-acetylgalactosaminyltransferase 4 Homo sapiens
3 Here, we report the direct carbohydrate binding of two GalNAc-transferase lectin domains, GalNAc-T4 and GalNAc-T2, representing isoforms reported to have distinct glycopeptide activity (GalNAc-T4) and isoforms without apparent distinct GalNAc-glycopeptide specificity (GalNAc-T2). N-acetylgalactosaminuronic acid polypeptide N-acetylgalactosaminyltransferase 4 Homo sapiens