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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
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Title[1H, 13H] NMR determination of the order of lobe loading of human transferrin with iron: Comparison with other metal ions
 
AuthorsSun, H2
Cox, MC2
Li, H2
Mason, AB1
Woodworth, RC1
Sadler, PJ2
 
Issue Date1998
 
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
 
CitationFebs Letters, 1998, v. 422 n. 3, p. 315-320 [How to Cite?]
DOI: http://dx.doi.org/10.1016/S0014-5793(98)00034-9
 
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.
 
ISSN0014-5793
2013 Impact Factor: 3.341
2013 SCImago Journal Rankings: 2.342
 
DOIhttp://dx.doi.org/10.1016/S0014-5793(98)00034-9
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorSun, H
 
dc.contributor.authorCox, MC
 
dc.contributor.authorLi, H
 
dc.contributor.authorMason, AB
 
dc.contributor.authorWoodworth, RC
 
dc.contributor.authorSadler, PJ
 
dc.date.accessioned2012-10-08T03:08:52Z
 
dc.date.available2012-10-08T03:08:52Z
 
dc.date.issued1998
 
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.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationFebs Letters, 1998, v. 422 n. 3, p. 315-320 [How to Cite?]
DOI: http://dx.doi.org/10.1016/S0014-5793(98)00034-9
 
dc.identifier.doihttp://dx.doi.org/10.1016/S0014-5793(98)00034-9
 
dc.identifier.epage320
 
dc.identifier.issn0014-5793
2013 Impact Factor: 3.341
2013 SCImago Journal Rankings: 2.342
 
dc.identifier.issue3
 
dc.identifier.pmid9498807
 
dc.identifier.scopuseid_2-s2.0-0032488671
 
dc.identifier.spage315
 
dc.identifier.urihttp://hdl.handle.net/10722/167593
 
dc.identifier.volume422
 
dc.languageeng
 
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
 
dc.publisher.placeNetherlands
 
dc.relation.ispartofFEBS Letters
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAluminum - Chemistry
 
dc.subject.meshAnimals
 
dc.subject.meshBismuth - Chemistry
 
dc.subject.meshCells, Cultured
 
dc.subject.meshCricetinae
 
dc.subject.meshFerric Compounds - Chemistry
 
dc.subject.meshGallium - Chemistry
 
dc.subject.meshHumans
 
dc.subject.meshIron - Chemistry
 
dc.subject.meshMagnetic Resonance Spectroscopy
 
dc.subject.meshMetals - Chemistry
 
dc.subject.meshProtein Binding
 
dc.subject.meshProtein Conformation
 
dc.subject.meshRecombinant Proteins - Chemistry - Genetics
 
dc.subject.meshTransferrin - Chemistry - Genetics
 
dc.title[1H, 13H] NMR determination of the order of lobe loading of human transferrin with iron: Comparison with other metal ions
 
dc.typeArticle
 
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Author Affiliations
  1. University of Vermont College of Medicine
  2. University of Edinburgh