Unravelling the Time Scale of Conformational Plasticity and Allostery in Glycan Recognition by Human Galectin‐1
Abstract: The interaction of human galectin‐1 with a variety of oligosaccharides, from di‐(N‐acetyllactosamine) to tetra‐saccharides (blood B type‐II antigen) has been scrutinized by using a combined approach of different NMR experiments, molecular dynamics (MD) simulations, and isothermal titration calorimetry. Ligand‐ and receptor‐based NMR experiments assisted by computational methods allowed proposing three‐dimensional structures for the different complexes, which explained the lack of enthalpy gain when increasing the chemical complexity of the glycan. Interestingly, and independently of the glycan ligand, the entropy term does not oppose the binding event, a rather unusual feature for protein‐sugar interactions. CLEANEX‐PM and relaxation dispersion experiments revealed that sugar binding affected residues far from the binding site and described significant changes in the dynamics of the protein. In particular, motions in the microsecond‐millisecond timescale in residues at the protein dimer interface were identified in the presence of high affinity ligands. The dynamic process was further explored by extensive MD simulations, which provided additional support for the existence of allostery in glycan recognition by human galectin‐1.
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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Unravelling the Time Scale of Conformational Plasticity and Allostery in Glycan Recognition by Human Galectin‐1 ; volume:26 ; number:67 ; year:2020 ; pages:15643-15653 ; extent:11
Chemistry - a European journal ; 26, Heft 67 (2020), 15643-15653 (gesamt 11)
- Urheber
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Bertuzzi, Sara
Gimeno, Ana
Núñez‐Franco, Reyes
Bernardo‐Seisdedos, Ganeko
Delgado, Sandra
Jiménez‐Osés, Gonzalo
Millet, Oscar
Jiménez‐Barbero, Jesús
Ardá, Ana
- DOI
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10.1002/chem.202003212
- URN
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urn:nbn:de:101:1-2022060416293897109569
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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15.08.2025, 07:24 MESZ
Datenpartner
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Bertuzzi, Sara
- Gimeno, Ana
- Núñez‐Franco, Reyes
- Bernardo‐Seisdedos, Ganeko
- Delgado, Sandra
- Jiménez‐Osés, Gonzalo
- Millet, Oscar
- Jiménez‐Barbero, Jesús
- Ardá, Ana
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