1suv

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==Overview==
==Overview==
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Iron, insoluble as free Fe(3+) and toxic as free Fe(2+), is distributed, through the body as Fe(3+) bound to transferrin (Tf) for delivery to cells, by endocytosis of its complex with transferrin receptor (TfR). Although, much is understood of the transferrin endocytotic cycle, little has been, uncovered of the molecular details underlying the formation of the, receptor-transferrin complex. Using cryo-electron microscopy, we have, produced a density map of the TfR-Tf complex at subnanometer resolution., An atomic model, obtained by fitting crystal structures of diferric Tf and, the receptor ectodomain into the map, shows that the Tf N-lobe is, sandwiched between the membrane and the TfR ectodomain and that the C-lobe, abuts the receptor helical domain. When Tf binds receptor, its N-lobe, moves by about 9 A with respect to its C-lobe. The structure of TfR-Tf, complex helps account for known differences in the iron-release properties, of free and receptor bound Tf.
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Iron, insoluble as free Fe(3+) and toxic as free Fe(2+), is distributed through the body as Fe(3+) bound to transferrin (Tf) for delivery to cells by endocytosis of its complex with transferrin receptor (TfR). Although much is understood of the transferrin endocytotic cycle, little has been uncovered of the molecular details underlying the formation of the receptor-transferrin complex. Using cryo-electron microscopy, we have produced a density map of the TfR-Tf complex at subnanometer resolution. An atomic model, obtained by fitting crystal structures of diferric Tf and the receptor ectodomain into the map, shows that the Tf N-lobe is sandwiched between the membrane and the TfR ectodomain and that the C-lobe abuts the receptor helical domain. When Tf binds receptor, its N-lobe moves by about 9 A with respect to its C-lobe. The structure of TfR-Tf complex helps account for known differences in the iron-release properties of free and receptor bound Tf.
==Disease==
==Disease==
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[[Category: Aisen, P.]]
[[Category: Aisen, P.]]
[[Category: Cheng, Y.]]
[[Category: Cheng, Y.]]
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[[Category: Harrison, S.C.]]
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[[Category: Harrison, S C.]]
[[Category: Walz, T.]]
[[Category: Walz, T.]]
[[Category: Zak, O.]]
[[Category: Zak, O.]]
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[[Category: protein complex]]
[[Category: protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:54:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:24 2008''

Revision as of 13:05, 21 February 2008


1suv

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Structure of Human Transferrin Receptor-Transferrin Complex

Contents

Overview

Iron, insoluble as free Fe(3+) and toxic as free Fe(2+), is distributed through the body as Fe(3+) bound to transferrin (Tf) for delivery to cells by endocytosis of its complex with transferrin receptor (TfR). Although much is understood of the transferrin endocytotic cycle, little has been uncovered of the molecular details underlying the formation of the receptor-transferrin complex. Using cryo-electron microscopy, we have produced a density map of the TfR-Tf complex at subnanometer resolution. An atomic model, obtained by fitting crystal structures of diferric Tf and the receptor ectodomain into the map, shows that the Tf N-lobe is sandwiched between the membrane and the TfR ectodomain and that the C-lobe abuts the receptor helical domain. When Tf binds receptor, its N-lobe moves by about 9 A with respect to its C-lobe. The structure of TfR-Tf complex helps account for known differences in the iron-release properties of free and receptor bound Tf.

Disease

Known diseases associated with this structure: Atransferrinemia OMIM:[190000], Iron deficiency anemia, susceptibility to OMIM:[190000]

About this Structure

1SUV is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the human transferrin receptor-transferrin complex., Cheng Y, Zak O, Aisen P, Harrison SC, Walz T, Cell. 2004 Feb 20;116(4):565-76. PMID:14980223

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