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000086442 0247_ $$2pmid$$apmid:18798567
000086442 0247_ $$2doi$$a10.1002/prot.22222
000086442 0247_ $$2ISSN$$a0887-3585
000086442 0247_ $$2ISSN$$a1097-0134
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000086442 037__ $$aPHPPUBDB-8735
000086442 041__ $$aeng
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000086442 1001_ $$aMaveyraud, L.
000086442 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000086442 245__ $$aStructural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra
000086442 260__ $$aNew York, NY$$bWiley-Liss$$c2008
000086442 300__ $$a89-103
000086442 3367_ $$00$$2EndNote$$aJournal Article
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000086442 440_0 $$0PERI:(DE-600)1475032-6$$aProteins: Struct. Funct. Bioinf.$$v75$$x0887-3585$$y1
000086442 500__ $$3Converted on 2013-05-30 12:43
000086442 500__ $$3Converted on 2013-06-21 19:20
000086442 520__ $$aBark of elderberry (Sambucus nigra) contains a galactose (Gal)/N-acetylgalactosamine (GalNAc)-specific lectin (SNA-II) corresponding to slightly truncated B-chains of a genuine Type-II ribosome-inactivating protein (Type-II RIPs, SNA-V), found in the same species. The three-dimensional X-ray structure of SNA-II has been determined in two distinct crystal forms, hexagonal and tetragonal, at 1.90 A and 1.35 A, respectively. In both crystal forms, the SNA-II molecule folds into two linked beta-trefoil domains, with an overall conformation similar to that of the B-chains of ricin and other Type-II RIPs. Glycosylation is observed at four sites along the polypeptide chain, accounting for 14 saccharide units. The high-resolution structures of SNA-II in complex with Gal and five Gal-related saccharides (GalNAc, lactose, alpha1-methylgalactose, fucose, and the carcinoma-specific Tn antigen) were determined at 1.55 A resolution or better. Binding is observed in two saccharide-binding sites for most of the sugars: a conserved aspartate residue interacts simultaneously with the O3 and O4 atoms of saccharides. In one of the binding sites, additional interactions with the protein involve the O6 atom. Analytical gel filtration, small angle X-ray scattering studies and crystal packing analysis indicate that, although some oligomeric species are present, the monomeric species predominate in solution.
000086442 536__ $$0G:(DE-H253)POF1-No-Ref-20130405$$aFS Beamline without reference (POF1-550)$$cPOF1-550$$fPOF I$$x0
000086442 588__ $$aDataset connected to Pubmed
000086442 650_2 $$2MeSH$$aAntigens, Tumor-Associated, Carbohydrate: chemistry
000086442 650_2 $$2MeSH$$aAntigens, Tumor-Associated, Carbohydrate: metabolism
000086442 650_2 $$2MeSH$$aBinding Sites
000086442 650_2 $$2MeSH$$aCrystallography, X-Ray
000086442 650_2 $$2MeSH$$aGalactose: analysis
000086442 650_2 $$2MeSH$$aGalactose: chemistry
000086442 650_2 $$2MeSH$$aGalactose: metabolism
000086442 650_2 $$2MeSH$$aPlant Lectins: chemistry
000086442 650_2 $$2MeSH$$aPlant Lectins: isolation & purification
000086442 650_2 $$2MeSH$$aPlant Lectins: metabolism
000086442 650_2 $$2MeSH$$aPolysaccharides: chemistry
000086442 650_2 $$2MeSH$$aProtein Binding
000086442 650_2 $$2MeSH$$aProtein Conformation
000086442 650_2 $$2MeSH$$aProtein Multimerization
000086442 650_2 $$2MeSH$$aRibosome Inactivating Proteins: chemistry
000086442 650_2 $$2MeSH$$aRibosome Inactivating Proteins: isolation & purification
000086442 650_2 $$2MeSH$$aRibosome Inactivating Proteins: metabolism
000086442 650_2 $$2MeSH$$aSambucus nigra: chemistry
000086442 650_2 $$2MeSH$$aSambucus nigra: metabolism
000086442 650_2 $$2MeSH$$aScattering, Small Angle
000086442 650_2 $$2MeSH$$aWood: chemistry
000086442 650_7 $$00$$2NLM Chemicals$$aAntigens, Tumor-Associated, Carbohydrate
000086442 650_7 $$00$$2NLM Chemicals$$aPlant Lectins
000086442 650_7 $$00$$2NLM Chemicals$$aPolysaccharides
000086442 650_7 $$00$$2NLM Chemicals$$aSambucus nigra lectins
000086442 650_7 $$00$$2NLM Chemicals$$aTn antigen
000086442 650_7 $$026566-61-0$$2NLM Chemicals$$aGalactose
000086442 650_7 $$0EC 3.2.2.22$$2NLM Chemicals$$aRibosome Inactivating Proteins
000086442 693__ $$0EXP:(DE-H253)Unknown-BL-20150101$$6EXP:(DE-H253)Unknown-BL-20150101$$fUnknown DESY Beamline$$x0
000086442 7001_ $$aNiwa, H.
000086442 7001_ $$aGuillet, V.
000086442 7001_ $$aSvergun, D. I.
000086442 7001_ $$aKonarev, P. V.
000086442 7001_ $$aPalmer, R. A.
000086442 7001_ $$aPeumans, W. J.
000086442 7001_ $$aRouge, P.
000086442 7001_ $$aVan Damme, E. J.
000086442 7001_ $$aReynolds, C. D.
000086442 7001_ $$aMourey, L.
000086442 773__ $$0PERI:(DE-600)1475032-6$$a10.1002/prot.22222$$gVol. 75, p. 89-103$$p89-103$$q75<89-103$$tProteins$$v75$$x0887-3585$$y2008
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000086442 9141_ $$a(c) 2008 Wiley-Liss, Inc., A Wiley Company$$y2008
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000086442 920_1 $$iEuropean Molecular Biology Laboratory$$kEMBL
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