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dc.contributor.authorHaselhorst, Thomasen_US
dc.contributor.authorWeimar, Thomasen_US
dc.contributor.authorPeters, Thomasen_US
dc.date.accessioned2017-05-03T12:21:35Z
dc.date.available2017-05-03T12:21:35Z
dc.date.issued2001en_US
dc.date.modified2008-02-14T08:12:00Z
dc.identifier.issn0002-7863en_US
dc.identifier.urihttp://hdl.handle.net/10072/16692
dc.description.abstractThe interaction of sialyl Lewis(x), Lewis(x), and a-L-Fuc-(1?3)-߭D-GlcNAc with isolectin A from Lotus tetragonolobus (LTL-A), and with Aleuria aurantia agglutinin (AAA) was studied using NMR experiments and surface plasmon resonance. Both lectins are specific for fucose residues. From NMR experiments it was concluded that a-L-Fuc-(1?3)-߭D-GlcNAc and Lewis(x) bound to both lectins, whereas sialyl Lewis(x) only bound to AAA. Increased line broadening of 1H NMR signals of the carbohydrate ligands upon binding to AAA and LTL-A suggested that AAA bound to the ligands more tightly. Further comparison of line widths showed that for both lectins binding strengths decreased from a-L-Fuc-(1?3)-߭D-GlcNAc to Lewis(x) and were lowest for sialyl Lewis(x). Surface plasmon resonance measurements were then employed to yield accurate dissociation constants. TrNOESY, QUIET-trNOESY, and trROESY experiments delivered bioactive conformations of the carbohydrate ligands, and STD NMR experiments allowed a precise epitope mapping of the carbohydrates bound to the lectins. The bioactive conformation of Lewis(x) bound to LTL-A, or AAA revealed an unusual orientation of the fucose residue, with negative values for both dihedral angles, F and ?, at the a(1?3)-glycosidic linkage. A similar distortion of the fucose orientation was also observed for sialyl Lewis(x) bound to AAA. From STD NMR experiments it followed that only the L-fucose residues are in intimate contact with the protein. Presumably steric interactions are responsible for locking the sialic acid residue of sialyl Lewis(x) in one out of many orientations that are present in aqueous solution. The sialic acid residue of sialyl Lewis(x) bound to AAA adopts an orientation similar to that in the corresponding sialyl Lewis(x)/E-selectin complex.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherAmerican Chemical Societyen_US
dc.publisher.placeEaston, Pa.en_US
dc.relation.ispartofpagefrom10705en_US
dc.relation.ispartofpageto10714en_US
dc.relation.ispartofissue43en_US
dc.relation.ispartofjournalJournal of the American Chemical Societyen_US
dc.relation.ispartofvolume123en_US
dc.subject.fieldofresearchcode270108en_US
dc.subject.fieldofresearchcode320302en_US
dc.subject.fieldofresearchcode270199en_US
dc.titleMolecular recognition of sialyl Lewis(x) and related saccharides by two lectinsen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2001
gro.hasfulltextNo Full Text


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