ArticleGlycobiology2016
Binding of polysaccharides to human galectin-3 at a noncanonical site in its carbohydrate recognition domain.
Article in Glycobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 70 citations in OpenAlex.
- Functional Specialization of Clathrin-Independent Endocytic Routes: Mechanisms and Cellular Roles.Traffic (Copenhagen, Denmark) · 2026Review
- Developing Galectin-3-Targeted Therapeutics in Diseases: Three Distinct Galectin-3 Segments for Targeting.Expert reviews in molecular medicine · 2026Review
- Galectin-3 induces neurodevelopmental apical-basal polarity and regulates gyrification.Science advances · 2025Article
- Pectin: Health-promoting properties as a natural galectin-3 inhibitor.Glycoconjugate journal · 2024Review
- Heterologous Interactions with Galectins and Chemokines and Their Functional Consequences.International journal of molecular sciences · 2023Review
- Targeting galectin-driven regulatory circuits in cancer and fibrosis.Nature reviews. Drug discovery · 2023Review
- Exploring multivalent carbohydrate-protein interactions by NMR.Chemical Society reviews · 2023Review
- Selectively Modified Lactose andInternational journal of molecular sciences · 2023Article
- Distinct features of the host-parasite interactions between nonadherent and adherent Trichomonas vaginalis isolates.PLoS neglected tropical diseases · 2023Article
- Galectin-1 and Galectin-3 in B-Cell Precursor Acute Lymphoblastic Leukemia.International journal of molecular sciences · 2022Article
- Targeting disordered-structured domain interactions in Galectin-3 based on NMR and enhanced MD.Biophysical journal · 2022Article
- MG-International journal of molecular sciences · 2022Article
- Experimental and Computational Models of Transport of Galectin-3 Through Glycosylated Matrix.Annals of biomedical engineering · 2022Article
- The Complex Biological Effects of Pectin: Galectin-3 Targeting as Potential Human Health Improvement?Biomolecules · 2022Review
- Inhibition of galectins in cancer: Biological challenges for their clinical application.Frontiers in immunology · 2022Review
- The marriage of chemokines and galectins as functional heterodimers.Cellular and molecular life sciences : CMLS · 2021Review
- Molecular dynamics simulations elucidate oligosaccharide recognition pathways by galectin-3 at atomic resolution.The Journal of biological chemistry · 2021Article
- Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells.International journal of molecular sciences · 2021Article
- Exploration of Galectin Ligands Displayed on Gram-Negative Respiratory Bacterial Pathogens with Different Cell Surface Architectures.Biomolecules · 2021Article
- Degraded Arabinogalactans and Their Binding Properties to Cancer-Associated Human Galectins.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Galectin-3 (Gal-3) is a multifunctional lectin, unique to galectins by the presence of a long N-terminal tail (NT) off of its carbohydrate recognition domain (CRD). Many previous studies have investigated binding of small carbohydrates to its CRD. Here, we used nuclear magnetic resonance spectroscopy ((15)N-(1)H heteronuclear single quantum coherence data) to assess binding of (15)N-Gal-3 (and truncated (15)N-Gal-3 CRD) to several, relatively large polysaccharides, including eight varieties of galactomannans (GMs), as well as a β(1 → 4)-polymannan and an α-branched mannan. Overall, we found that these polysaccharides with a larger carbohydrate footprint interact primarily with a noncanonical carbohydrate-binding site on the F-face of the Gal-3 CRD β-sandwich, and to a less extent, if at all, with the canonical carbohydrate-binding site on the S-face. While there is no evidence for interaction with the NT itself, it does appear that the NT somehow mediates stronger interactions between the Gal-3 CRD and the GMs. Significant Gal-3 resonance broadening observed during polysaccharide titrations indicates that interactions occur in the intermediate exchange regime, and analysis of these data allows estimation of affinities and stoichiometries that range from 4 × 10(4) to 12 × 10(4) M(-1) per site and multiple sites per polysaccharide, respectively. We also found that lactose can still bind to the CRD S-face of GM-bound Gal-3, with the binding of one ligand attenuating affinity of the other. These data are compared with previous results on Gal-1, revealing differences and similarities. They also provide research direction to the development of these polysaccharides as galectin-targeting therapeutics in the clinic.
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