Understanding the structural specificity of Tn antigen for its receptor: an NMR solution study
| Autor: | Fulvio Uggeri, Nicola D'Amelio, Anna Coslovi, Sergio Paoletti, Marco Rossi |
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| Přispěvatelé: | D'Amelio, Nicola, Coslovi, Anna, Rossi, Marco, Uggeri, Fulvio, Paoletti, Sergio |
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Lectins Molecular recognition NMR spectroscopy Tn antigen Vicia villosa Antigens Tumor-Associated Carbohydrate Hydrogen Bonding Isomerism Magnetic Resonance Spectroscopy Plant Lectins Protein Conformation Serine Solutions Substrate Specificity Biochemistry Analytical Chemistry Organic Chemistry Carbohydrate Molecular model Stereochemistry Epitope Protein structure Models Solution Antigens chemistry.chemical_classification Chemistry Plant Lectin Tumor-Associated Molecular General Medicine Nuclear magnetic resonance spectroscopy Amino acid Lectin Heteronuclear single quantum coherence spectroscopy |
| Zdroj: | Carbohydrate Research. 351:114-120 |
| ISSN: | 0008-6215 |
| Popis: | The present work aims at understanding the structural basis of the biological recognition of Tn antigen (GalNAc-α-O-L-Ser), a specific epitope expressed by tumor cells, and the role of its amino acidic moiety in the interaction with its receptor (the isolectin B4 extracted from Vicia villosa). An NMR structural characterization of the α and β anomers, based on J couplings and molecular modeling revealed a structure in very good agreement with data reported in literature for variants of the same molecules. In order to demonstrate the involvement of the amino acid in the ligand–receptor recognition, also GalNAc-α-O-D-Ser was studied; the change in the stereochemistry is in fact expected to impact on the interaction only in case the serine is part of the epitope. Relaxation properties in the presence of the receptor clearly indicated a selective recognition of the natural L form, probably due to the formation of a water-mediated hydrogen bond with Asn 129 of the protein. |
| Databáze: | OpenAIRE |
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