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Atomic and Specificity Details of Mucin 1 <i>O</i>-Glycosylation Process by Multiple Polypeptide GalNAc-Transferase Isoforms Unveiled by NMR and Molecular Modeling

Helena Coelho, Matilde de las Rivas, Ana Sofia Grosso, Ana Diniz, Cátia O. Soares, Rodrigo A. Francisco, Jorge S. Dias, Ismael Compañón, Lingbo Sun, Yoshiki Narimatsu, Sergey Y. Vakhrushev, Henrik Clausen, Eurico J. Cabrita, Jesús Jiménez‐Barbero, Francisco Corzana, Ramón Hurtado‐Guerrero, Filipa Marcelo

2022JACS Au35 citationsDOIOpen Access PDF

Abstract

, which highlights the relevance of GalNAc-T4 in the glycosylation of this epitope. Finally, the NMR methodology established herein can be extended to other glycosyltransferases, such as C1GalT1 and ST6GalNAc-I, to determine the specificity toward complex mucin acceptor substrates.

Topics & Concepts

GlycosylationGene isoformTandem repeatGlycanBiochemistryChemistryLectinTransferaseMucinBiologyGlycoproteinEnzymeGeneGenomeGlycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisGalectins and Cancer Biology
Atomic and Specificity Details of Mucin 1 <i>O</i>-Glycosylation Process by Multiple Polypeptide GalNAc-Transferase Isoforms Unveiled by NMR and Molecular Modeling | Litcius