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dc.contributor.authorBohari, Mohammad H
dc.contributor.authorYu, Xing
dc.contributor.authorZick, Yehiel
dc.contributor.authorBlanchard, Helen
dc.date.accessioned2017-11-27T05:05:34Z
dc.date.available2017-11-27T05:05:34Z
dc.date.issued2016
dc.identifier.issn2045-2322
dc.identifier.doi10.1038/srep39556
dc.identifier.urihttp://hdl.handle.net/10072/100861
dc.description.abstractGlycosphingolipids are ubiquitous cell surface molecules undertaking fundamental cellular processes. Lacto-N-tetraose (LNT) and lacto-N-neotetraose (LNnT) are the representative core structures for lacto- and neolacto-series glycosphingolipids. These glycolipids are the carriers to the blood group antigen and human natural killer antigens mainly found on blood cells, and are also principal components in human milk, contributing to infant health. The β-galactoside recognising galectins mediate various cellular functions of these glycosphingolipids. We report crystallographic structures of the galectin-8 N-terminal domain (galectin-8N) in complex with LNT and LNnT. We reveal the first example in which the non-reducing end of LNT binds to the primary binding site of a galectin, and provide a structure-based rationale for the significant ten-fold difference in binding affinities of galectin-8N toward LNT compared to LNnT, such a magnitude of difference not being observed for any other galectin. In addition, the LNnT complex showed that the unique Arg59 has ability to adopt a new orientation, and comparison of glycerol- and lactose-bound galectin-8N structures reveals a minimum atomic framework for ligand recognition. Overall, these results enhance our understanding of glycosphingolipids interactions with galectin-8N, and highlight a structure-based rationale for its significantly different affinity for components of biologically relevant glycosphingolipids.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherNature Macmillan
dc.relation.ispartofpagefrom1
dc.relation.ispartofpageto12
dc.relation.ispartofissue39556
dc.relation.ispartofjournalScientific Reports
dc.relation.ispartofvolume6
dc.subject.fieldofresearchCellular Interactions (incl. Adhesion, Matrix, Cell Wall)
dc.subject.fieldofresearchcode060106
dc.titleStructure-based rationale for differential recognition of lacto- and neolacto- series glycosphingolipids by the N-terminal domain of human galectin-8
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomics
gro.rights.copyright© The Author(s) 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
gro.hasfulltextFull Text
gro.griffith.authorBlanchard, Helen
gro.griffith.authorYu, Xing
gro.griffith.authorBohari, Mohammad


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