Source:http://linkedlifedata.com/resource/pubmed/id/16343946
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2005-12-19
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pubmed:abstractText |
Most organisms depend on iron as a co-factor for proteins catalyzing redox reactions. Iron is, however, a difficult element for cells to deal with, as it is insoluble in its ferric (Fe3+) form and potentially toxic in its ferrous (Fe2+) form. Thus, in vertebrates iron is transported through the circulation bound to transferrin (Tf) and delivered to cells through an endocytotic cycle involving the transferrin receptor (TfR). We have previously presented a model for the Tf-TfR complex in its iron-bearing form, the diferric transferrin (dTf)-TfR complex [Cheng, Y., Zak, O., Aisen, P., Harrison, S.C., Walz, T., 2004. Structure of the human transferrin receptor-transferrin complex. Cell 116, 565-576]. We have now calculated a single particle reconstruction for the complex in its iron-free form, the apo-transferrin (apoTf)-TfR complex. The same density map was obtained by aligning raw particle images or class averages of the vitrified apoTf-TfR complex to reference models derived from the structures of the dTf-TfR or apoTf-TfR complex. We were unable to improve the resolution of the apoTf-TfR density map beyond 16A, most likely because of significant structural variability of Tf in its iron-free state. The density map does, however, support the model for the apoTf-TfR we previously proposed based on the dTf-TfR complex structure, and it suggests that receptor-bound apoTf prefers to adopt an open conformation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/apotransferrin,
http://linkedlifedata.com/resource/pubmed/chemical/diferric transferrin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1047-8477
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
152
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
204-10
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:16343946-Apoproteins,
pubmed-meshheading:16343946-Cryoelectron Microscopy,
pubmed-meshheading:16343946-Humans,
pubmed-meshheading:16343946-Imaging, Three-Dimensional,
pubmed-meshheading:16343946-Models, Molecular,
pubmed-meshheading:16343946-Peptide Fragments,
pubmed-meshheading:16343946-Protein Binding,
pubmed-meshheading:16343946-Receptors, Transferrin,
pubmed-meshheading:16343946-Recombinant Proteins,
pubmed-meshheading:16343946-Transferrin
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pubmed:year |
2005
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pubmed:articleTitle |
Single particle reconstruction of the human apo-transferrin-transferrin receptor complex.
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pubmed:affiliation |
Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. ycheng@hms.harvard.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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