File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: The low pKa value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin

TitleThe low pKa value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin
Authors
KeywordsAnion binding
BHK, baby-hamster kidney cells
Heteronuclear single-quantum coherence nuclear magnetic resonance
hTF, human serum transferrin
hTF/2N, recombinant N-lobe of human transferrin comprising residues 1-337
pK a
Transferrin
Tyrosine
Issue Date2004
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2004, v. 573 n. 1-3, p. 181-185 How to Cite?
Abstract2D NMR-pH titrations were used to determine pKa values for four conserved tyrosine residues, Tyr45, Tyr85, Tyr96 and Tyr188, in human transferrin. The low pKa of Tyr188 is due to the fact that the iron-binding ligand interacts with Lys206 in open-form and with Lys296 in the closed-form of the protein. Our current results also confirm the anion binding of sulfate and arsenate to transferrin and further suggest that Tyr188 is the actual binding site for the anions in solution. These data indicate that Tyr188 is a critical residue not only for iron binding but also for chelator binding and iron release in transferrin. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Persistent Identifierhttp://hdl.handle.net/10722/48523
ISSN
2014 Impact Factor: 3.169
2014 SCImago Journal Rankings: 1.569
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSun, Xen_HK
dc.contributor.authorSun, Hen_HK
dc.contributor.authorGe, Ren_HK
dc.contributor.authorRichter, Men_HK
dc.contributor.authorWoodworth, RCen_HK
dc.contributor.authorMason, ABen_HK
dc.contributor.authorHe, QYen_HK
dc.date.accessioned2008-05-22T04:16:08Z-
dc.date.available2008-05-22T04:16:08Z-
dc.date.issued2004en_HK
dc.identifier.citationFebs Letters, 2004, v. 573 n. 1-3, p. 181-185en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48523-
dc.description.abstract2D NMR-pH titrations were used to determine pKa values for four conserved tyrosine residues, Tyr45, Tyr85, Tyr96 and Tyr188, in human transferrin. The low pKa of Tyr188 is due to the fact that the iron-binding ligand interacts with Lys206 in open-form and with Lys296 in the closed-form of the protein. Our current results also confirm the anion binding of sulfate and arsenate to transferrin and further suggest that Tyr188 is the actual binding site for the anions in solution. These data indicate that Tyr188 is a critical residue not only for iron binding but also for chelator binding and iron release in transferrin. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.en_HK
dc.format.extent381136 bytes-
dc.format.extent254114 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypeapplication/pdf-
dc.languageengen_HK
dc.languagefreen_HK
dc.languagegeren_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.rightsF E B S Letters. Copyright © Elsevier BV.en_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectAnion bindingen_HK
dc.subjectBHK, baby-hamster kidney cellsen_HK
dc.subjectHeteronuclear single-quantum coherence nuclear magnetic resonanceen_HK
dc.subjecthTF, human serum transferrinen_HK
dc.subjecthTF/2N, recombinant N-lobe of human transferrin comprising residues 1-337en_HK
dc.subjectpK aen_HK
dc.subjectTransferrinen_HK
dc.subjectTyrosineen_HK
dc.titleThe low pKa value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-5793&volume=573&issue=1-3&spage=181&epage=185&date=2004&atitle=The+low+pKa+value+of+iron-binding+ligand+tyr188+and+its+implication+in+iron+release+and+anion+binding+of+human+transferrinen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1016/j.febslet.2004.07.076en_HK
dc.identifier.pmid15327995en_HK
dc.identifier.scopuseid_2-s2.0-4344645436en_HK
dc.identifier.hkuros98457-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-4344645436&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume573en_HK
dc.identifier.issue1-3en_HK
dc.identifier.spage181en_HK
dc.identifier.epage185en_HK
dc.identifier.isiWOS:000223697200031-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridSun, X=8906547400en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.scopusauthoridGe, R=7005525090en_HK
dc.identifier.scopusauthoridRichter, M=7402643053en_HK
dc.identifier.scopusauthoridWoodworth, RC=7006217057en_HK
dc.identifier.scopusauthoridMason, AB=7203074416en_HK
dc.identifier.scopusauthoridHe, QY=34770287900en_HK
dc.identifier.citeulike3814034-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats