Structural Basis of Oligomannose Recognition by the Pterocarpus angolensis Seed Lectin

Loris, Remy; Walle, Ivo Van; Greve, Henri De; Beeckmans, Sonia; Deboeck, Francine; Wyns, Lode; Bouckaert, Julie

doi:10.1016/j.jmb.2003.11.043

Cited by 48 publications

(63 citation statements)

References 44 publications

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“…Although we predict that the affinities for these alternative binding modes would be slightly lower (probably similar to that of a monosaccharide), the binding mode observed in the crystal is not expected to be all dominating. Our earlier work also showed that isolated Mana(1-3)[Mana(1-6)] Man and Mana(1-2)Man each bind in a single binding mode (Loris et al, 2004) while two are expected. For Mana(1-2)Man, the 5-times higher binding constant (compared to Man) could still explain the observation of an apparent single-binding mode in the crystal structure.…”

Section: Alternative Binding Modesmentioning

confidence: 70%

“…The crystals contain a dimer of PAL in their asymmetric unit, the two subunits of which will be termed A and B. The overall structure of the PAL dimer has previously been described in detail (Loris et al, 2003(Loris et al, , 2004 and remains unaltered in the complexes presented in this article. These two subunits are chemically identical and show only minor conformational differences that are irrelevant for carbohydrate binding.…”

Section: Overall Structurementioning

confidence: 96%

“…The carbohydrate-binding site of subunit A is involved in crystal packing and therefore limits the conformations that are accessible to the bound carbohydrate. After the desoaking step (see ''Materials and Methods''), a molecule of Mana(1-3)Man remains bound (Loris et al, 2005), but in a number of cases this can still be substituted by a different carbohydrate ligand if the concentration of the replacing ligand is sufficiently high (Loris et al, 2003(Loris et al, , 2004Buts et al, 2006). The interactions and carbohydrate conformations observed in this binding site then have to be interpreted as situations that are possible in solution, but not necessarily reflecting the dominant one.…”

Section: Overall Structurementioning

confidence: 99%

“…This resulted in a clear picture of how this lectin recognizes mono-, di-, and trisaccharides (Loris et al, 2004) as well as complex-type oligosaccharides and how its structure, stability, and activity respond to demetalization . Here we report the crystal structures of PAL in complex with a series of high Man ligands ranging from Man-5 to Man-9.…”

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confidence: 99%

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How a Plant Lectin Recognizes High Mannose Oligosaccharides

et al. 2007

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The crystal structure of Pterocarpus angolensis seed lectin is presented in complex with a series of high mannose (Man) oligosaccharides ranging from Man-5 to Man-9. Despite that several of the nine Man residues of Man-9 have the potential to bind in the monosaccharide-binding site, all oligomannoses are bound in the same unique way, employing the tetrasaccharide sequence Mana(1-2)Mana(1-6)[Mana(1-3)]Mana(1-. Isothermal titration calorimetry titration experiments using Man-5, Man-9, and the Man-9-containing glycoprotein soybean (Glycine max) agglutinin as ligands confirm the monovalence of Man-9 and show a 4-times higher affinity for Man-9 when it is presented to P. angolensis seed lectin in a glycoprotein context.For already a long time, plants are known to express lectins in relatively large amounts in their storage organs (seeds, rhizomes) and in lower concentrations in their vegetative parts. The seeds from legume plants have traditionally been excellent sources for lectins of a variety of specificities. For several decades, the legume lectin family has served as the model system of choice for the study of protein-carbohydrate recognition (Sharon and Lis, 1990; Loris et al., 1998). Many principles have been discovered first for legume lectin family members and were later confirmed for other families of carbohydrate-recognizing proteins (Loris, 2002). The legume lectin family covers the widest possible range of carbohydrate specificities among all known lectin families. Variations of the lengths, sequences, and conformations of five loops that constitute the carbohydrate-binding site determine mono-and oligosaccharide specificity in a complex way (Sharma and Surolia, 1997;Loris et al., 1998). Avidity and higher order specificity are generated via a variety of quaternary structures leading to the formation of homogeneous cross-linked lattices (Bhattacharyya et al., 1988;Sacchettini et al., 2001). The past decade has provided a wealth of structural and thermodynamic data that provide insight on how oligosaccharide specificity, quaternary structure, and metal binding cooperate to generate a variety of biological effects.Despite the wealth of data obtained from x-ray crystallography, relatively few structures of lectins in complex with large oligosaccharides are available.

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Section: Alternative Binding Modesmentioning

confidence: 70%

Section: Overall Structurementioning

confidence: 96%

Section: Overall Structurementioning

confidence: 99%

mentioning

confidence: 99%

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How a Plant Lectin Recognizes High Mannose Oligosaccharides

et al. 2007

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“…the agglutinin from Pterocarpus angolensis seed (PAL). 4 Crystallography and thermodynamic studies demonstrated high affinity for both oligomannose N-glycans and for biantennary complex type, correlated with the presence of an unusually extended binding region close to the primary binding site (17)(18)(19)(20).…”

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A Lectin from Platypodium elegans with Unusual Specificity and Affinity for Asymmetric Complex N-Glycans

Benevides

Ganne

Simoes

et al. 2012

Journal of Biological Chemistry

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Background: Legume lectins with new glycan specificity can be discovered in the Dalbergieae tribe. Results: We determined the sequence, specificity, and crystal structures of a new Man/Glc lectin (PELa) from Platypodium elegans seeds. Conclusion: The unusual affinity of PELa for asymmetrical complex N-glycans is related to the extended binding site and conformational constraints on oligosaccharides. Significance: Dalbergieae lectins are of interest for biotechnological applications.

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Structural Features of Lectins and Their Binding Sites

Loris

2009

Bioinformatics for Glycobiology and Glycomics

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Structural Basis of Oligomannose Recognition by the Pterocarpus angolensis Seed Lectin

Cited by 48 publications

References 44 publications

How a Plant Lectin Recognizes High Mannose Oligosaccharides

How a Plant Lectin Recognizes High Mannose Oligosaccharides

A Lectin from Platypodium elegans with Unusual Specificity and Affinity for Asymmetric Complex N-Glycans

Structural Features of Lectins and Their Binding Sites

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