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dc.contributor.authorHadley, B
dc.contributor.authorMaggioni, A
dc.contributor.authorAshikov, A
dc.contributor.authorDay, CJ
dc.contributor.authorHaselhorst, T
dc.contributor.authorTiralongo, J
dc.date.accessioned2017-05-03T14:17:01Z
dc.date.available2017-05-03T14:17:01Z
dc.date.issued2014
dc.identifier.issn2001-0370
dc.identifier.doi10.1016/j.csbj.2014.05.003
dc.identifier.urihttp://hdl.handle.net/10072/65551
dc.description.abstractThe proteomes of eukaryotes, bacteria and archaea are highly diverse due, in part, to the complex post-translational modification of protein glycosylation. The diversity of glycosylation in eukaryotes is reliant on nucleotide sugar transporters to translocate specific nucleotide sugars that are synthesised in the cytosol and nucleus, into the endoplasmic reticulum and Golgi apparatus where glycosylation reactions occur. Thirty years of research utilising multidisciplinary approaches has contributed to our current understanding of NST function and structure. In this review, the structure and function, with reference to various disease states, of several NSTs including the UDP-galactose, UDP-N-acetylglucosamine, UDP-N-acetylgalactosamine, GDP-fucose, UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose and CMP-sialic acid transporters will be described. Little is known regarding the exact structure of NSTs due to difficulties associated with crystallising membrane proteins. To date, no three-dimensional structure of any NST has been elucidated. What is known is based on computer predictions, mutagenesis experiments, epitope-tagging studies, in-vitro assays and phylogenetic analysis. In this regard the best-characterised NST to date is the CMP-sialic acid transporter (CST). Therefore in this review we will provide the current state-of-play with respect to the structure-function relationship of the (CST). In particular we have summarised work performed by a number groups detailing the affect of various mutations on CST transport activity, efficiency, and substrate specificity.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent1029887 bytes
dc.format.extent1063236 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeSweden
dc.relation.ispartofstudentpublicationY
dc.relation.ispartofpagefrom23
dc.relation.ispartofpageto32
dc.relation.ispartofissue16
dc.relation.ispartofjournalComputational and Structural Biotechnology Journal
dc.relation.ispartofvolume10
dc.rights.retentionY
dc.subject.fieldofresearchStructural Biology (incl. Macromolecular Modelling)
dc.subject.fieldofresearchReceptors and Membrane Biology
dc.subject.fieldofresearchNumerical and Computational Mathematics
dc.subject.fieldofresearchComputation Theory and Mathematics
dc.subject.fieldofresearchcode060112
dc.subject.fieldofresearchcode060110
dc.subject.fieldofresearchcode0103
dc.subject.fieldofresearchcode0802
dc.titleStructure and function of nucleotide sugar transporters: Current progress
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by/3.0/
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomics
gro.rights.copyright© 2014 Hadley et al. Published by Elsevier B.V. on behalf of the Research Network of Computational and Structural Biotechnology. This is an open access article under the CC BY 3.0 license (http://creativecommons.org/licenses/by/3.0/) that permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
gro.date.issued2015-03-20T04:35:26Z
gro.hasfulltextFull Text
gro.griffith.authorHaselhorst, Thomas E.
gro.griffith.authorDay, Christopher J.
gro.griffith.authorMaggioni, Andrea
gro.griffith.authorTiralongo, Joe
gro.griffith.authorHadley, Barbara J.


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