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Article: [1H, 13H] NMR determination of the order of lobe loading of human transferrin with iron: Comparison with other metal ions

Title[1H, 13H] NMR determination of the order of lobe loading of human transferrin with iron: Comparison with other metal ions
Authors
Issue Date1998
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 1998, v. 422 n. 3, p. 315-320 How to Cite?
Abstract
Human serum transferrin (hTF) is a single-chain bilobal glycoprotein (80 kDa) which transports Fe3+ and a variety of other metal ions in blood. Only diferric transferrin, not the apo-protein, binds strongly to transferrin receptors and is taken up by cells via receptor-mediated endocytosis. We show here that 2D [1H, 13C] NMR studies of recombinant ε[13C]Met-hTF allow the order of lobe loading with various metal ions, including Fe3+, to be determined. In particular, the resonance for Met-464, a residue in the hydrophobic patch of helix 5, is very sensitive to iran binding in the C-lobe. The selectivity of lobe loading with Fe3+ is compared to loading with Fe2+ (which binds as Fe3+), Al3+, Ga3+ and Bi3+. Similar changes in shifts of the Met residues are observed for these metal ions, suggesting that they induce similar conformational changes in the protein.
Persistent Identifierhttp://hdl.handle.net/10722/167593
ISSN
2013 Impact Factor: 3.341
2013 SCImago Journal Rankings: 2.342
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSun, Hen_US
dc.contributor.authorCox, MCen_US
dc.contributor.authorLi, Hen_US
dc.contributor.authorMason, ABen_US
dc.contributor.authorWoodworth, RCen_US
dc.contributor.authorSadler, PJen_US
dc.date.accessioned2012-10-08T03:08:52Z-
dc.date.available2012-10-08T03:08:52Z-
dc.date.issued1998en_US
dc.identifier.citationFebs Letters, 1998, v. 422 n. 3, p. 315-320en_US
dc.identifier.issn0014-5793en_US
dc.identifier.urihttp://hdl.handle.net/10722/167593-
dc.description.abstractHuman serum transferrin (hTF) is a single-chain bilobal glycoprotein (80 kDa) which transports Fe3+ and a variety of other metal ions in blood. Only diferric transferrin, not the apo-protein, binds strongly to transferrin receptors and is taken up by cells via receptor-mediated endocytosis. We show here that 2D [1H, 13C] NMR studies of recombinant ε[13C]Met-hTF allow the order of lobe loading with various metal ions, including Fe3+, to be determined. In particular, the resonance for Met-464, a residue in the hydrophobic patch of helix 5, is very sensitive to iran binding in the C-lobe. The selectivity of lobe loading with Fe3+ is compared to loading with Fe2+ (which binds as Fe3+), Al3+, Ga3+ and Bi3+. Similar changes in shifts of the Met residues are observed for these metal ions, suggesting that they induce similar conformational changes in the protein.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_US
dc.relation.ispartofFEBS Lettersen_US
dc.subject.meshAluminum - Chemistryen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBismuth - Chemistryen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCricetinaeen_US
dc.subject.meshFerric Compounds - Chemistryen_US
dc.subject.meshGallium - Chemistryen_US
dc.subject.meshHumansen_US
dc.subject.meshIron - Chemistryen_US
dc.subject.meshMagnetic Resonance Spectroscopyen_US
dc.subject.meshMetals - Chemistryen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshRecombinant Proteins - Chemistry - Geneticsen_US
dc.subject.meshTransferrin - Chemistry - Geneticsen_US
dc.title[1H, 13H] NMR determination of the order of lobe loading of human transferrin with iron: Comparison with other metal ionsen_US
dc.typeArticleen_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0014-5793(98)00034-9en_US
dc.identifier.pmid9498807en_US
dc.identifier.scopuseid_2-s2.0-0032488671en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032488671&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume422en_US
dc.identifier.issue3en_US
dc.identifier.spage315en_US
dc.identifier.epage320en_US
dc.identifier.isiWOS:000072096300007-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridSun, H=7404827446en_US
dc.identifier.scopusauthoridCox, MC=7401826848en_US
dc.identifier.scopusauthoridLi, H=14023043100en_US
dc.identifier.scopusauthoridMason, AB=7203074416en_US
dc.identifier.scopusauthoridWoodworth, RC=7006217057en_US
dc.identifier.scopusauthoridSadler, PJ=7103024488en_US

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