Ontology highlight
ABSTRACT:
SUBMITTER: Pedersen JW
PROVIDER: S-EPMC3173194 | biostudies-other | 2011 Sep
REPOSITORIES: biostudies-other
Pedersen Johannes W JW Bennett Eric P EP Schjoldager Katrine T-B G KT Meldal Morten M Holmér Andreas P AP Blixt Ola O Cló Emiliano E Levery Steven B SB Clausen Henrik H Wandall Hans H HH
The Journal of biological chemistry 20110715 37
UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (GalNAc-Ts) constitute a family of up to 20 transferases that initiate mucin-type O-glycosylation. The transferases are structurally composed of catalytic and lectin domains. Two modes have been identified for the selection of glycosylation sites by GalNAc-Ts: confined sequence recognition by the catalytic domain alone, and concerted recognition of acceptor sites and adjacent GalNAc-glycosylated sites by the catalytic and lectin domains ...[more]