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dc.contributor.authorHaselhorst, T
dc.contributor.authorWilson, JC
dc.contributor.authorThomson, RJ
dc.contributor.authorMcAtamney, S
dc.contributor.authorMenting, JG
dc.contributor.authorCoppel, RL
dc.contributor.authorvon Itzstein, M
dc.contributor.editorEE Lattman
dc.date.accessioned2017-05-03T11:05:54Z
dc.date.available2017-05-03T11:05:54Z
dc.date.issued2004
dc.date.modified2012-02-10T02:56:34Z
dc.identifier.issn0887-3585
dc.identifier.doi10.1002/prot.20143
dc.identifier.urihttp://hdl.handle.net/10072/5067
dc.description.abstractSaturation transfer difference (STD) 1H NMR experiments were used to probe the epitope binding characteristics of the sialidase [EC 3.2.1.18] from the bacterium Vibrio cholerae, the causative agent of cholera. Binding preferences were investigated for N-acetylneuraminic acid (Neu5Ac, 1), the product of the sialidase catalytic reaction, for the known sialidase inhibitor 5-acetamido-2,6-anhydro-3,5-dideoxy-D-glycero-D-galacto-non-2-enoic acid (Neu5Ac2en, 2), and for the uronic acid-based Neu5Ac2en mimetic iso-propyl 2-acetamido-2,4-dideoxy--L-threo-hex-4-enopyranosiduronic acid (3), in which the native glycerol side-chain of Neu5Ac2en is replaced with an O-iso-propyl ether. The STD experiments provided evidence, supporting previous studies, that Neu5Ac (1) binds to the sialidase as the -anomer. Docking experiments using DOCK (version 4.0.1) revealed further information regarding the binding characteristics of the enzyme active site in complex with Neu5Ac2en (2) and the Neu5Ac2en mimetic (3), indicating an expected dominant interaction of the acetamide moiety with the protein.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoen_US
dc.publisherWiley-Liss, Inc
dc.publisher.placeUSA
dc.publisher.urihttp://www3.interscience.wiley.com/journal/36176/home
dc.relation.ispartofpagefrom346
dc.relation.ispartofpageto353
dc.relation.ispartofjournalProteins: Structure, Function and Bioinformatics
dc.relation.ispartofvolume56
dc.subject.fieldofresearchHistory and Archaeology
dc.subject.fieldofresearchMathematical Sciences
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchInformation and Computing Sciences
dc.subject.fieldofresearchcode21
dc.subject.fieldofresearchcode01
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode08
dc.titleSaturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 2004 John Wiley & Sons, Ltd. Self-archiving of the author-manuscript version is not yet supported by this publisher. Please refer to the journal link for access to the definitive, published version or contact the author for more information.
gro.date.issued2004
gro.hasfulltextNo Full Text
gro.griffith.authorvon Itzstein, Mark
gro.griffith.authorThomson, Robin J.
gro.griffith.authorWilson, Jenny C.
gro.griffith.authorHaselhorst, Thomas E.
gro.griffith.authorBlyth, Sarah


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