The conformation of the C-glycosyl analogue of N-acetyl-lactosamine in the free state and bound to a toxic plant agglutinin and human adhesion/growth-regulatory galectin-1

Garcı́a-Aparicio, Vı́ctor; Sollogoub, Matthieu; Blériot, Yves; Colliou, Virginie; André, Sabine; Asensio, Juan Luis; Cañada, F. Javier; Gabius, Hans‐Joachim; Sînaÿ, Pierre; Jiménez‐Barbero, Jesús

doi:10.1016/j.carres.2007.02.034

Cited by 21 publications

(6 citation statements)

References 47 publications

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“…4, magenta and red). These dihedral angles were stable throughout the simulations with values of~60 and 20 for V and J, respectively, which correspond to low-energy conformations of the disaccharides as reported previously (33). Interaction energies between galectin-1 and the two disaccharides were computed with CHARMM ( Fig.…”

Section: Of Galectin-1 With Lactose N-acetyllactosaminesupporting

confidence: 67%

NMR and MD Investigations of Human Galectin-1/Oligosaccharide Complexes

Meynier

Feracci

Espéli

et al. 2009

Biophysical Journal

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The specific recognition of carbohydrates by lectins plays a major role in many cellular processes. Galectin-1 belongs to a family of 15 structurally related beta-galactoside binding proteins that are able to control a variety of cellular events, including cell cycle regulation, adhesion, proliferation, and apoptosis. The three-dimensional structure of galectin-1 has been solved by x-ray crystallography in the free form and in complex with various carbohydrate ligands. In this work, we used a combination of two-dimensional NMR titration experiments and molecular-dynamics simulations with explicit solvent to study the mode of interaction between human galectin-1 and five galactose-containing ligands. Isothermal titration calorimetry measurements were performed to determine their affinities for galectin-1. The contribution of the different hexopyranose units in the protein-carbohydrate interaction was given particular consideration. Although the galactose moiety of each oligosaccharide is necessary for binding, it is not sufficient by itself. The nature of both the reducing sugar in the disaccharide and the interglycosidic linkage play essential roles in the binding to human galectin-1.

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Section: Of Galectin-1 With Lactose N-acetyllactosaminesupporting

confidence: 67%

NMR and MD Investigations of Human Galectin-1/Oligosaccharide Complexes

Meynier

Feracci

Espéli

et al. 2009

Biophysical Journal

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“…As previously revealed by NMR analysis using C-lactose (57) as well as follow-up studies by the same group (58,59), the 3-OH or 4-OH of the reducing terminal monosaccharide, e.g., Glc(NAc)/ Gal(NAc)/Man(NAc), always takes a gauche position in the case of Galβ-equatorial when the glycosidic bond is in a syn configuration. When galectins bind to their ligands (e.g., lactose), the glycosidic bond of lactose shows two types of rotations φ and Ψ.…”

Section: Simultaneous Determination Of Dissociation Constant (Kd)mentioning

confidence: 59%

Carbohydrate-Binding Specificity of Human Galectins: An Overview by Frontal Affinity Chromatography

Iwaki

Hirabayashi

2018

Trends in Glycoscience and Glycotechnology

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To understand the biological functions of lectins, it is important to investigate their sugar-binding specificity. Although galectins are characterized as β-galactoside-binding proteins comprising evolutionarily conserved amino-acid sequences, they have significantly divergent specificities depending on their individual carbohydrate-recognition domains (CRDs). Of the various methods available to analyze lectin-glycan interactions, frontal affinity chromatography is unique in that it provides a quantitative set of dissociation constants (K d's) between immobilized lectins and a panel of (>100) fluorescently labeled oligosaccharides. In this article, we provide an overview of the features of galectin specificities with a focus on human galectins based on published data. From the data obtained, comprehensive features of individual CRDs can be systematically understood in terms of branching, and 3′-modifications including sialylation, sulfation, αGal/GalNAc substitutions, β1-3Gal extension, and N-acetyllactosamine repeats. Additionally, we analyze evolutionarily more distant galectin molecules of non-human origins. These findings provide not only basic knowledge but also useful information for their applications: e.g., for engineering superior galectins improved in their specificity and affinity and developing galectin-targeted drugs. A. Introduction: Transforming Lectinomics Lectins are a group of carbohydrate-binding proteins with diverse structures and specificities. Recent analysis revealed that the number of protein families of lectins and those involving lectin domains is almost 50 (1). This is surprising considering that the number of representative lectin families at the end of 20th century was only 10: R-type lectins (ricin B chain-like lectins) of β-trefoil fold, L-type lectins (legume lectin-like lectins) of β-sandwich fold (jellyroll), GNA (Galanthus nivalis agglutinin)-related lectins of β-prism II fold, jacalin-related lectins (mJRLs and gJRLs) of β-prism I fold, hevein-like lectins (chitin-binding lectins) of hevein-type cystineknot motif, C-type lectins (Ca-dependent-type animal lectins) of Ctype α/β fold, galectins (β-galactoside-binding lectins), siglecs (sialic acid-binding immunoglobulin-like lectins), hyaladhesins (hyaluronan-binding proteins) of C-type α/β fold, and pentraxins (a class of pattern recognition receptors involved in innate immunity) of β-sandwich fold (jellyroll). The latest members of new lectin families include the 17-kDa α-D-galactose-binding lectin from the Mediterranean mussel Mytilus galloprovincialis termed MytiLec 1) (2) and a 15.5-kDa mannose-specific lectin from the oyster Crassostrea gigas termed CGL1 (3). Lectin domains are also known as carbohydraterecognition domains (CRDs) in hydrolytic enzymes, typically belonging to the R-type lectin family (4). They are termed "carbohydrate-binding modules" (CBMs) in the framework of Carbohydrate-Active enZymes (CAZy), with family numbers CBM 1-84 (http:// www.cazy.org/Carbohydrate-Binding-Modules.html). Lectin domains are also fo...

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“…An additional monitoring of T 1 values demonstrated that the selective T 1 value of H1-Gal strongly decreases when passing from the free to the bound state, again indicating ligand binding. [38]…”

Section: Characterization Of Protein-carbohydrate Interactions By Nmrmentioning

confidence: 99%

Protein-Carbohydrate Interactions Studied by NMR: From Molecular Recognition to Drug Design

Fernández‐Alonso¹,

Díaz²,

Berbís³

et al. 2012

CPPS

121

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Diseases that result from infection are, in general, a consequence of specific interactions between a pathogenic organism and the cells. The study of host-pathogen interactions has provided insights for the design of drugs with therapeutic properties. One area that has proved to be promising for such studies is the constituted by carbohydrates which participate in biological processes of paramount importance. On the one hand, carbohydrates have shown to be information carriers with similar, if not higher, importance than traditionally considered carriers as amino acids and nucleic acids. On the other hand, the knowledge on molecular recognition of sugars by lectins and other carbohydrate-binding proteins has been employed for the development of new biomedical strategies. Biophysical techniques such as X-Ray crystallography and NMR spectroscopy lead currently the investigation on this field. In this review, a description of traditional and novel NMR methodologies employed in the study of sugar-protein interactions is briefly presented in combination with a palette of NMR-based studies related to biologically and/or pharmaceutically relevant applications.

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The conformation of the C-glycosyl analogue of N-acetyl-lactosamine in the free state and bound to a toxic plant agglutinin and human adhesion/growth-regulatory galectin-1

Cited by 21 publications

References 47 publications

NMR and MD Investigations of Human Galectin-1/Oligosaccharide Complexes

NMR and MD Investigations of Human Galectin-1/Oligosaccharide Complexes

Carbohydrate-Binding Specificity of Human Galectins: An Overview by Frontal Affinity Chromatography

Protein-Carbohydrate Interactions Studied by NMR: From Molecular Recognition to Drug Design

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