2hau

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Template:STRUCTURE 2hau

Contents 1 Apo-Human Serum Transferrin (Non-Glycosylated) 2 Disease 3 Function 4 About this Structure 5 See Also 6 Reference

Apo-Human Serum Transferrin (Non-Glycosylated)

Template:ABSTRACT PUBMED 16793765

Disease

[TRFE_HUMAN] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:209300]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.^[1][2]

Function

[TRFE_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.

About this Structure

2hau is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Molecular Playground/Transferrin
• Transferrin

Reference

• Wally J, Halbrooks PJ, Vonrhein C, Rould MA, Everse SJ, Mason AB, Buchanan SK. The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding. J Biol Chem. 2006 Aug 25;281(34):24934-44. Epub 2006 Jun 22. PMID:16793765 doi:10.1074/jbc.M604592200

1. ↑ Beutler E, Gelbart T, Lee P, Trevino R, Fernandez MA, Fairbanks VF. Molecular characterization of a case of atransferrinemia. Blood. 2000 Dec 15;96(13):4071-4. PMID:11110675
2. ↑ Knisely AS, Gelbart T, Beutler E. Molecular characterization of a third case of human atransferrinemia. Blood. 2004 Oct 15;104(8):2607. PMID:15466165 doi:10.1182/blood-2004-05-1751