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Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
Published on: June 28, 2024
Serine versus threonine glycosylation with α-O-GalNAc: unexpected selectivity in their molecular recognition with
David Madariaga1, Nuria Martínez-Sáez, Víctor J Somovilla
1Departamento de Química, Centro de investigación en Síntesis Química, Universidad de La Rioja, C/Madre de Dios 51, 26006 Logroño (Spain).
Abstract:
The molecular recognition of several glycopeptides bearing Tn antigen (α-O-GalNAc-Ser or α-O-GalNAc-Thr) in their structure by three lectins with affinity for this determinant has been analysed. The work yields remarkable results in terms of epitope recognition, showing that the underlying amino acid of Tn (serine or threonine) plays a key role in the molecular recognition. In fact, while Soybean agglutinin and Vicia villosa agglutinin lectins prefer Tn-threonine, Helix pomatia agglutinin shows a higher affinity for the glycopeptides carrying Tn-serine. The different conformational behaviour of the two Tn biological entities, the residues of the studied glycopeptides in the close proximity to the Tn antigen and the topology of the binding site of the lectins are at the origin of these differences.
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