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Serine versus Threonine Glycosylation with α‐ O ‐GalNAc: Unexpected Selectivity in Their Molecular Recognition with Lectins
Author(s) -
Madariaga David,
MartínezSáez Nuria,
Somovilla Víctor J.,
GarcíaGarcía Laura,
Berbis M. Álvaro,
ValeroGónzalez Jessika,
MartínSantamaría Sonsoles,
HurtadoGuerrero Ramon,
Asensio Juan L.,
JiménezBarbero Jesús,
Avenoza Alberto,
Busto Jesús H.,
Corzana Francisco,
Peregrina Jesús M.
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201403700
Subject(s) - threonine , soybean agglutinin , biochemistry , glycopeptide , serine , epitope , lectin , glycosylation , agglutinin , chemistry , biology , peanut agglutinin , stereochemistry , antigen , phosphorylation , genetics , antibiotics
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.