Serine versus Threonine Glycosylation with α‐O‐GalNAc: Unexpected Selectivity in Their Molecular Recognition with Lectins |
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| Authors: | Víctor J Somovilla Laura García‐García M Álvaro Berbis Jessika Valero‐Gónzalez Dr Sonsoles Martín‐Santamaría Ramon Hurtado‐Guerrero Dr Juan L Asensio Dr Jesús Jiménez‐Barbero Dr Alberto Avenoza Dr Jesús H Busto Dr Francisco Corzana Dr Jesús M Peregrina |
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| Institution: | 1. Departamento de Química, Centro de investigación en Síntesis Química, Universidad de La Rioja, C/Madre de Dios 51, 26006 Logro?o (Spain);2. Centro de Investigaciones Biológicas, CSIC, 28040 Madrid (Spain);3. Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, BIFI‐IQFR (CSIC) 50018 Zaragoza (Spain);4. Departamento de Química, Universidad San Pablo CEU, 28003 Madrid (Spain);5. Instituto de Química Orgánica General, CSIC, 28006 Madrid (Spain) |
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| 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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| Keywords: | conformation analysis glycopeptides molecular dynamics molecular recognition mucin |
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