Home > Publications database > Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra > print

001     86442
005     20250731122923.0
024 7 _ |a pmid:18798567
|2 pmid
024 7 _ |a 10.1002/prot.22222
|2 doi
024 7 _ |a 0887-3585
|2 ISSN
024 7 _ |a 1097-0134
|2 ISSN
024 7 _ |a WOS:000263546600008
|2 WOS
024 7 _ |a altmetric:7786670
|2 altmetric
024 7 _ |a openalex:W2149106632
|2 openalex
037 _ _ |a PHPPUBDB-8735
041 _ _ |a eng
082 _ _ |a 540
100 1 _ |a Maveyraud, L.
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra
260 _ _ |a New York, NY
|b Wiley-Liss
|c 2008
300 _ _ |a 89-103
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a article
|2 DRIVER
336 7 _ |a Journal Article
|m journal
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
440 _ 0 |a Proteins: Struct. Funct. Bioinf.
|v 75
|y 1
|x 0887-3585
|0 PERI:(DE-600)1475032-6
500 _ _ |3 Converted on 2013-05-30 12:43
500 _ _ |3 Converted on 2013-06-21 19:20
520 _ _ |a 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.
536 _ _ |0 G:(DE-H253)POF1-No-Ref-20130405
|f POF I
|x 0
|c POF1-550
|a FS Beamline without reference (POF1-550)
588 _ _ |a Dataset connected to Pubmed
650 _ 2 |2 MeSH
|a Antigens, Tumor-Associated, Carbohydrate: chemistry
650 _ 2 |2 MeSH
|a Antigens, Tumor-Associated, Carbohydrate: metabolism
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Galactose: analysis
650 _ 2 |2 MeSH
|a Galactose: chemistry
650 _ 2 |2 MeSH
|a Galactose: metabolism
650 _ 2 |2 MeSH
|a Plant Lectins: chemistry
650 _ 2 |2 MeSH
|a Plant Lectins: isolation & purification
650 _ 2 |2 MeSH
|a Plant Lectins: metabolism
650 _ 2 |2 MeSH
|a Polysaccharides: chemistry
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protein Multimerization
650 _ 2 |2 MeSH
|a Ribosome Inactivating Proteins: chemistry
650 _ 2 |2 MeSH
|a Ribosome Inactivating Proteins: isolation & purification
650 _ 2 |2 MeSH
|a Ribosome Inactivating Proteins: metabolism
650 _ 2 |2 MeSH
|a Sambucus nigra: chemistry
650 _ 2 |2 MeSH
|a Sambucus nigra: metabolism
650 _ 2 |2 MeSH
|a Scattering, Small Angle
650 _ 2 |2 MeSH
|a Wood: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Antigens, Tumor-Associated, Carbohydrate
650 _ 7 |0 0
|2 NLM Chemicals
|a Plant Lectins
650 _ 7 |0 0
|2 NLM Chemicals
|a Polysaccharides
650 _ 7 |0 0
|2 NLM Chemicals
|a Sambucus nigra lectins
650 _ 7 |0 0
|2 NLM Chemicals
|a Tn antigen
650 _ 7 |0 26566-61-0
|2 NLM Chemicals
|a Galactose
650 _ 7 |0 EC 3.2.2.22
|2 NLM Chemicals
|a Ribosome Inactivating Proteins
693 _ _ |0 EXP:(DE-H253)Unknown-BL-20150101
|f Unknown DESY Beamline
|x 0
|6 EXP:(DE-H253)Unknown-BL-20150101
700 1 _ |a Niwa, H.
700 1 _ |a Guillet, V.
700 1 _ |a Svergun, D. I.
700 1 _ |a Konarev, P. V.
700 1 _ |a Palmer, R. A.
700 1 _ |a Peumans, W. J.
700 1 _ |a Rouge, P.
700 1 _ |a Van Damme, E. J.
700 1 _ |a Reynolds, C. D.
700 1 _ |a Mourey, L.
773 _ _ |0 PERI:(DE-600)1475032-6
|a 10.1002/prot.22222
|g Vol. 75, p. 89-103
|p 89-103
|q 75<89-103
|t Proteins
|v 75
|x 0887-3585
|y 2008
909 C O |o oai:bib-pubdb1.desy.de:86442
|p VDB
910 1 _ |0 I:(DE-HGF)0
|a Externes Institut
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913 1 _ |0 G:(DE-HGF)POF1-540
|9 G:(DE-H253)POF1-No-Ref-20130405
|v Kondensierte Materie
|x 0
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|4 G:(DE-HGF)POF
|1 G:(DE-HGF)POF1-550
|3 G:(DE-HGF)POF1
|2 G:(DE-HGF)POF1-500
|b Struktur der Materie
|l Großgeräte für die Forschung mit Photonen, Neutronen, Ionen
914 1 _ |a (c) 2008 Wiley-Liss, Inc., A Wiley Company
|y 2008
915 _ _ |a JCR/ISI refereed
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915 _ _ |a No Author Disambiguation
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920 _ 1 |k EMBL
|i European Molecular Biology Laboratory
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|l European Molecular Biology Laboratory
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920 _ _ |k 001
980 _ _ |a PHPPUBDB
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980 _ _ |a ConvertedRecord

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