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1SUV

Structure of Human Transferrin Receptor-Transferrin Complex

Summary for 1SUV
Entry DOI10.2210/pdb1suv/pdb
Related1A8E 1CX8 1JNF
DescriptorTransferrin receptor protein 1, Serotransferrin, N-lobe, Serotransferrin, C-lobe, ... (5 entities in total)
Functional Keywordsprotein complex, metal transport
Biological sourceHomo sapiens (human)
More
Cellular locationCell membrane; Single-pass type II membrane protein. Transferrin receptor protein 1, serum form: Secreted: P02786
Secreted: P02787
Total number of polymer chains6
Total formula weight293127.06
Authors
Cheng, Y.,Zak, O.,Aisen, P.,Harrison, S.C.,Walz, T. (deposition date: 2004-03-26, release date: 2004-04-13, Last modification date: 2024-10-30)
Primary citationCheng, Y.,Zak, O.,Aisen, P.,Harrison, S.C.,Walz, T.
Structure of the Human Transferrin Receptor-Transferrin Complex
Cell(Cambridge,Mass.), 116:565-576, 2004
Cited by
PubMed Abstract: 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.
PubMed: 14980223
DOI: 10.1016/S0092-8674(04)00130-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.5 Å)
Structure validation

226707

数据于2024-10-30公开中

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