TY  - JOUR
AU  - Maveyraud, L.
AU  - Niwa, H.
AU  - Guillet, V.
AU  - Svergun, D. I.
AU  - Konarev, P. V.
AU  - Palmer, R. A.
AU  - Peumans, W. J.
AU  - Rouge, P.
AU  - Van Damme, E. J.
AU  - Reynolds, C. D.
AU  - Mourey, L.
AU  - DESY
TI  - Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra
JO  - Proteins
VL  - 75
SN  - 0887-3585
CY  - New York, NY
PB  - Wiley-Liss
M1  - PHPPUBDB-8735
SP  - 89-103
PY  - 2008
AB  - Bark of elderberry (Sambucus nigra) contains a galactose (Gal)/N-acetylgalactosamine (GalNAc)-specific lectin (SNA-II) corresponding to slightly truncated B-chains of a genuine Type-II ribosome-inactivating protein (Type-II RIPs, SNA-V), found in the same species. The three-dimensional X-ray structure of SNA-II has been determined in two distinct crystal forms, hexagonal and tetragonal, at 1.90 A and 1.35 A, respectively. In both crystal forms, the SNA-II molecule folds into two linked beta-trefoil domains, with an overall conformation similar to that of the B-chains of ricin and other Type-II RIPs. Glycosylation is observed at four sites along the polypeptide chain, accounting for 14 saccharide units. The high-resolution structures of SNA-II in complex with Gal and five Gal-related saccharides (GalNAc, lactose, alpha1-methylgalactose, fucose, and the carcinoma-specific Tn antigen) were determined at 1.55 A resolution or better. Binding is observed in two saccharide-binding sites for most of the sugars: a conserved aspartate residue interacts simultaneously with the O3 and O4 atoms of saccharides. In one of the binding sites, additional interactions with the protein involve the O6 atom. Analytical gel filtration, small angle X-ray scattering studies and crystal packing analysis indicate that, although some oligomeric species are present, the monomeric species predominate in solution.
KW  - Antigens, Tumor-Associated, Carbohydrate: chemistry
KW  - Antigens, Tumor-Associated, Carbohydrate: metabolism
KW  - Binding Sites
KW  - Crystallography, X-Ray
KW  - Galactose: analysis
KW  - Galactose: chemistry
KW  - Galactose: metabolism
KW  - Plant Lectins: chemistry
KW  - Plant Lectins: isolation & purification
KW  - Plant Lectins: metabolism
KW  - Polysaccharides: chemistry
KW  - Protein Binding
KW  - Protein Conformation
KW  - Protein Multimerization
KW  - Ribosome Inactivating Proteins: chemistry
KW  - Ribosome Inactivating Proteins: isolation & purification
KW  - Ribosome Inactivating Proteins: metabolism
KW  - Sambucus nigra: chemistry
KW  - Sambucus nigra: metabolism
KW  - Scattering, Small Angle
KW  - Wood: chemistry
KW  - Antigens, Tumor-Associated, Carbohydrate (NLM Chemicals)
KW  - Plant Lectins (NLM Chemicals)
KW  - Polysaccharides (NLM Chemicals)
KW  - Sambucus nigra lectins (NLM Chemicals)
KW  - Tn antigen (NLM Chemicals)
KW  - Galactose (NLM Chemicals)
KW  - Ribosome Inactivating Proteins (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:18798567
UR  - <Go to ISI:>//WOS:000263546600008
DO  - DOI:10.1002/prot.22222
UR  - https://bib-pubdb1.desy.de/record/86442
ER  -