Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus 1 1Edited by R. Huber

Hamelryck, Thomas; Loris, Remy; Bouckaert, Julie; Dao‐Thi, Minh‐Hoa; Strecker, Gérard; Imberty, Anne; Fernandez, Elias J.; Wyns, Lode; Etzler, Marilynn E.

doi:10.1006/jmbi.1998.2534

Cited by 116 publications

(52 citation statements)

References 72 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The CϭO group is hydrogen bonded to the NH backbone of Ala 106 . This orientation of GalNAc, together with specific hydrogen bond and hydrophobic interactions of the N-acetyl group, is similar to that observed in the crystal structures of Dolichos biflorus seed lectin (13) and Robinia pseudoacacia bark lectin (32).…”

Section: Structural Basis For the Specificity Differences Between Gs supporting

confidence: 83%

Isolectins I-A and I-B of Griffonia(Bandeiraea) simplicifolia

Lescar

Loris

Mitchell

et al. 2002

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Seeds from the African legume shrub Griffonia simplicifolia contain several lectins. Among them the tetrameric lectin GS I-B 4 has strict specificity for terminal ␣Gal residues, whereas the closely related lectin GS I-A 4 can also bind to ␣GalNAc. These two lectins are commonly used as markers in histology or for research in xenotransplantation. To elucidate the basis for the fine difference in specificity, the amino acid sequences of both lectins have been determined and show 89% identity. The crystal structure of GS I-B 4 , determined at 2.5-Å resolution, reveals a new quaternary structure that has never been observed in other legume lectins. An unexpected loss of both Ca

show abstract

Section: Structural Basis For the Specificity Differences Between Gs supporting

confidence: 83%

Isolectins I-A and I-B of Griffonia(Bandeiraea) simplicifolia

Lescar

Loris

Mitchell

et al. 2002

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…1b, the tetramer can be seen both as an association of two canonical dimers, or alternatively as two DB58-like dimers (37). When comparing the two potential dimer interfaces of MAL, it becomes clear that both of them could occur in solution.…”

Section: Resultsmentioning

confidence: 99%

An Unusual Carbohydrate Binding Site Revealed by the Structures of Two Maackia amurensis Lectins Complexed with Sialic Acid-containing Oligosaccharides

Imberty¹,

Gautier²,

Lescar³

et al. 2000

Journal of Biological Chemistry

Self Cite

138

122

View full text Add to dashboard Cite

Seeds from the legume tree Maackia amurensis contain two lectins that can agglutinate different blood cell types. Their specificity toward sialylated oligosaccharides is unique among legume lectins; the leukoagglutinin preferentially binds to sialyllactosamine (␣NeuAc-(2-3)␤Gal(1-4)␤GlcNAc), whereas the hemagglutinin displays higher affinity for a disialylated tetrasaccharide (␣NeuAc(2-3)␤Gal(1-3)[␣NeuAc(2-6)]␣GalNAc). The three-dimensional structure of the complex between M. amurensis leukoagglutinin and sialyllactose has been determined at 2.75-Å resolution using x-ray crystallography. The carbohydrate binding site consists of a deep cleft that accommodates the three carbohydrate residues of the sialyllactose. The central galactose sits in the primary binding site in an orientation that has not been observed previously in other legume lectins. The carboxyl group of sialic acid establishes a salt bridge with a lysine side chain. The glucose residue is very efficiently docked between two tyrosine aromatic rings. The complex between M. amurensis hemagglutinin and a disialylated tetrasaccharide could be modeled from the leukoagglutinin/sialyllactose crystal structure. The substitution of one tyrosine by an alanine residue is responsible for the difference in fine specificity between the two isolectins. Comparison with other legume lectins indicates that oligosaccharide specificity within this family is achieved by the recycling of structural loops in different combinations.

show abstract

“…2; Gallego del Sol, F., Chornet, J. J. C., & Cavada, B. S. PDBcode: 2GDF; to be published) [4,15,[32][33][34][35][36][37][38][39][40][41][42]. A sequence alignment of the sequenced peptides of CRLII against other legume lectin sequence displays a similarity of 53% and 44% with the galactose-specific lectins VML and Rob, respectively (Fig.…”

Section: Protein Sequence and Biochemical Characterizationmentioning

confidence: 94%

“…2 Phylogenetic analysis based on legume lectins sequence alignment. The protein sequence alignment made among partial CRLII sequence with legume seed lectins: CRLI [15], Dgran [35], Dioclea guianensis lectin (Dgui) [37], Dioclea violacea lectin (DVL; Gallego del Sol, F., Chornet, J. J. C., & Cavada, B. S. PDBcode: 2GDF; to be published), Dioclea lehmanii lectin (DLLI) [4], Canavalia gladiata lectin (CGL) [38], ConA [30], ConBr [34], Acacia farnesiana lectin-like protein (AFAL) [39], PHAL [40], PHA [36], Dolichos biflorus lectin (DBL) [41], VML [32], Rob [33], and Dolichos lablab lectin (Dlab) [42]. The alignment and phylogram was generated using CLUSTALW web program Protein Crystallization and X-ray Data Collection…”

Section: Protein Sequence and Biochemical Characterizationmentioning

confidence: 99%

Purification, Characterization, and Preliminary X-Ray Diffraction Analysis of a Lactose-Specific Lectin from Cymbosema roseum Seeds

Rocha

Moreno

Delatorre

et al. 2008

Appl Biochem Biotechnol

View full text Add to dashboard Cite

The unique carbohydrate-binding property of lectins makes them invaluable tools in biomedical research. Here, we report the purification, partial primary structure, carbohydrate affinity characterization, crystallization, and preliminary X-ray diffraction analysis of a lactose-specific lectin from Cymbosema roseum seeds (CRLII). Isolation and purification of CRLII was performed by a single step using a Sepharose-4B-lactose affinity chromatography column. The carbohydrate affinity characterization was carried using assays for hemagglutination activity and inhibition. CRLII showed hemagglutinating activity toward rabbit erythrocytes. O-glycoproteins from mucine mucopolysaccharides showed the most potent inhibition capacity at a minimum concentration of 1.2 microg mL(-1). Protein sequencing by mass spectrometry was obtained by the digestion of CRLII with trypsin, Glu-C, and AspN. CRLII partial protein sequence exhibits 46% similarity with the ConA-like alpha chain precursor. Suitable protein crystals were obtained with the hanging-drop vapor-diffusion method with 8% ethylene glycol, 0.1 M Tris-HCl pH 8.5, and 11% PEG 8,000. The monoclinic crystals belong to space group P2(1) with unit cell parameters a = 49.4, b = 89.6, and c = 100.8 A.

show abstract

Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus 1 1Edited by R. Huber

Cited by 116 publications

References 72 publications

Isolectins I-A and I-B of Griffonia(Bandeiraea) simplicifolia

Isolectins I-A and I-B of Griffonia(Bandeiraea) simplicifolia

An Unusual Carbohydrate Binding Site Revealed by the Structures of Two Maackia amurensis Lectins Complexed with Sialic Acid-containing Oligosaccharides

Purification, Characterization, and Preliminary X-Ray Diffraction Analysis of a Lactose-Specific Lectin from Cymbosema roseum Seeds

Contact Info

Product

Resources

About