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- Publisher Website: 10.1038/srep00999
- Scopus: eid_2-s2.0-84871947083
- PMID: 23256035
- WOS: WOS:000312489900002
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Article: Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe
Title | Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe |
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Authors | |
Issue Date | 2012 |
Publisher | Nature Publishing Group. The Journal's web site is located at http://www.nature.com/srep/index.html |
Citation | Scientific Reports, 2012, v. 2, p. Article no. 999 How to Cite? |
Abstract | Human serum transferrin (hTF) binds Fe(III) tightly but reversibly, and delivers it to cells via a receptor-mediated endocytosis process. The metal-binding and release result in significant conformational changes of the protein. Here, we report the crystal structures of diferric-hTF (Fe N Fe C-hTF) and bismuth-bound hTF (Bi N Fe C-hTF) at 2.8 and 2.4 Å resolutions respectively. Notably, the N-lobes of both structures exhibit unique 'partially-opened' conformations between those of the apo-hTF and holo-hTF. Fe(III) and Bi(III) in the N-lobe coordinate to, besides anions, only two (Tyr95 and Tyr188) and one (Tyr188) tyrosine residues, respectively, in contrast to four residues in the holo-hTF. The C-lobe of both structures are fully closed with iron coordinating to four residues and a carbonate. The structures of hTF observed here represent key conformers captured in the dynamic nature of the transferrin family proteins and provide a structural basis for understanding the mechanism of metal uptake and release in transferrin families. © 2012 Macmillan Publishers Limited. All rights reserved. |
Persistent Identifier | http://hdl.handle.net/10722/184478 |
ISSN | 2023 Impact Factor: 3.8 2023 SCImago Journal Rankings: 0.900 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Yang, N | - |
dc.contributor.author | Zhang, H | - |
dc.contributor.author | Wang, M | - |
dc.contributor.author | Hao, Q | - |
dc.contributor.author | Sun, H | - |
dc.date.accessioned | 2013-07-15T09:49:08Z | - |
dc.date.available | 2013-07-15T09:49:08Z | - |
dc.date.issued | 2012 | - |
dc.identifier.citation | Scientific Reports, 2012, v. 2, p. Article no. 999 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | http://hdl.handle.net/10722/184478 | - |
dc.description.abstract | Human serum transferrin (hTF) binds Fe(III) tightly but reversibly, and delivers it to cells via a receptor-mediated endocytosis process. The metal-binding and release result in significant conformational changes of the protein. Here, we report the crystal structures of diferric-hTF (Fe N Fe C-hTF) and bismuth-bound hTF (Bi N Fe C-hTF) at 2.8 and 2.4 Å resolutions respectively. Notably, the N-lobes of both structures exhibit unique 'partially-opened' conformations between those of the apo-hTF and holo-hTF. Fe(III) and Bi(III) in the N-lobe coordinate to, besides anions, only two (Tyr95 and Tyr188) and one (Tyr188) tyrosine residues, respectively, in contrast to four residues in the holo-hTF. The C-lobe of both structures are fully closed with iron coordinating to four residues and a carbonate. The structures of hTF observed here represent key conformers captured in the dynamic nature of the transferrin family proteins and provide a structural basis for understanding the mechanism of metal uptake and release in transferrin families. © 2012 Macmillan Publishers Limited. All rights reserved. | - |
dc.language | eng | - |
dc.publisher | Nature Publishing Group. The Journal's web site is located at http://www.nature.com/srep/index.html | - |
dc.relation.ispartof | Scientific Reports | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.title | Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe | - |
dc.type | Article | - |
dc.identifier.email | Yang, N: yangnan@hku.hk | - |
dc.identifier.email | Zhang, H: hzhang20@hku.hk | - |
dc.identifier.email | Hao, Q: qhao@hku.hk | - |
dc.identifier.email | Sun, H: hsun@hku.hk | - |
dc.identifier.authority | Zhang, H=rp00306 | - |
dc.identifier.authority | Hao, Q=rp01332 | - |
dc.identifier.authority | Sun, H=rp00777 | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1038/srep00999 | - |
dc.identifier.pmid | 23256035 | - |
dc.identifier.pmcid | PMC3525939 | - |
dc.identifier.scopus | eid_2-s2.0-84871947083 | - |
dc.identifier.hkuros | 215978 | - |
dc.identifier.volume | 2 | - |
dc.identifier.spage | Article no. 999 | - |
dc.identifier.epage | Article no. 999 | - |
dc.identifier.isi | WOS:000312489900002 | - |
dc.publisher.place | United Kingdom | - |
dc.identifier.issnl | 2045-2322 | - |