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dc.contributor.authorBlanchard, Helenen_US
dc.contributor.authorCollins, Patricken_US
dc.contributor.authorI.P.J. Hidari, Kazuyaen_US
dc.date.accessioned2017-04-04T19:07:36Z
dc.date.available2017-04-04T19:07:36Z
dc.date.issued2007en_US
dc.identifier.issn09074449en_US
dc.identifier.doi10.1107/S090744490605270Xen_US
dc.identifier.urihttp://hdl.handle.net/10072/15546
dc.description.abstractGalectin-3 is a multifunctional carbohydrate-binding protein with roles in cancer progression. Besides carbohydrate-dependent extracellular functions, galectin-3 participates in carbohydrate-independent intracellular signalling pathways, including apoptosis, via protein-protein interactions, some engaging the carbohydrate-binding groove. When ligands bind within this site conformational rearrangements are induced and therefore information of un-liganded galectin-3 is valuable for structure-based drug-design. Removal of co-crystallised lactose from the human galectin-3 carbohydrate-recognition domain was achieved via crystal soaking, but took weeks, despite low affinity. Pre-soaking to remove lactose enabled subsequent binding of cryo-protectant glycerol, whereas when lactose was not removed a priori then the glycerol could not displace it over the short cryo-soak timeframe. Slow diffusion of lactose removal from crystals contrasts glycerol entering within minutes. The importance of removal of incumbent ligands prior to attempts to introduce alternative ligands is indicated, even for proteins exhibiting low affinity for ligands, and has significance for ligand exchange in structure based drug desigen_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_US
dc.languageEnglishen_US
dc.language.isoen_US
dc.publisherBlackwell Munksgaarden_US
dc.publisher.placeDenmarken_US
dc.relation.ispartofstudentpublicationNen_US
dc.relation.ispartofpagefrom415en_US
dc.relation.ispartofpageto419en_US
dc.relation.ispartofjournalActa Crystallographica. Section D: Biological Crystallographyen_US
dc.relation.ispartofvolumeD63en_US
dc.rights.retentionYen_US
dc.subject.fieldofresearchcode250502en_US
dc.titleSlow diffusion of lactose out of galectin-3 crystals monitored by X-ray crystallography: possible implications for ligand-exchange protocolsen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomicsen_US
gro.date.issued2015-01-30T00:42:46Z
gro.hasfulltextNo Full Text


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