The two domains of human galectin-8 bind sialyl- and fucose-containing oligosaccharides in an independent manner. A 3D view by using NMR
| Autor: | Reyes Núñez-Franco, Marcos Gómez-Redondo, Gonzalo Jiménez-Osés, Sandra Delgado, Ana Gimeno, Jesús Jiménez-Barbero, Ana Ardá |
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| Přispěvatelé: | European Commission |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Stereochemistry Supramolecular chemistry chain Synergistic combination 010402 general chemistry 01 natural sciences Biochemistry Genetics and Molecular Biology (miscellaneous) Biochemistry Fucose Epitope 03 medical and health sciences chemistry.chemical_compound Molecular dynamics galectin-8 oligosaccharides Molecular Biology NMR 3. Good health 0104 chemical sciences Galectin-8 Chemistry 030104 developmental biology chemistry Chemistry (miscellaneous) affinity recognition protein |
| Zdroj: | Addi. Archivo Digital para la Docencia y la Investigación instname Rsc Chemical Biology RSC Chemical Biology RIUR. Repositorio Institucional de la Universidad de La Rioja |
| Popis: | The interaction of human galectin-8 and its two separate N-terminal and C-terminal carbohydrate recognition domains (CRD) to their natural ligands has been analysed using a synergistic combination of experimental NMR and ITC methods, and molecular dynamics simulations. Both domains bind the minimal epitopes N-acetyllactosamine (1) and Galβ1–3GalNAc (2) in a similar manner. However, the N-terminal and C-terminal domains show exquisite and opposing specificity to bind either Neu5Ac- or Fuc-containing ligands, respectively. Moreover, the addition of the high-affinity ligands specific for one of the CRDs does not make any effect on the binding at the alternative one. Thus, the two CRDs behave independently and may simultaneously target different molecular entities to promote clustering through the generation of supramolecular assemblies. NMR, ITC, and MD data show that the two domains of human galectin-8 independently recognize sialyl- and fucosyl-containing glycans. |
| Databáze: | OpenAIRE |
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