1ryo
From Proteopedia
(Difference between revisions)
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| - | [[Image:1ryo.png|left|200px]] | ||
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{{STRUCTURE_1ryo| PDB=1ryo | SCENE= }} | {{STRUCTURE_1ryo| PDB=1ryo | SCENE= }} | ||
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===Human serum transferrin, N-lobe bound with oxalate=== | ===Human serum transferrin, N-lobe bound with oxalate=== | ||
| + | {{ABSTRACT_PUBMED_15123433}} | ||
| - | + | ==Disease== | |
| + | [[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[http://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref><ref>PMID:15466165</ref> | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/TRFE_HUMAN 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:015123433</ref><references group="xtra"/> | + | <ref group="xtra">PMID:015123433</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Adams, T E.]] | [[Category: Adams, T E.]] | ||
Revision as of 12:05, 24 March 2013
Contents |
Human serum transferrin, N-lobe bound with oxalate
Template:ABSTRACT PUBMED 15123433
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
1ryo is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Halbrooks PJ, Mason AB, Adams TE, Briggs SK, Everse SJ. The oxalate effect on release of iron from human serum transferrin explained. J Mol Biol. 2004 May 21;339(1):217-26. PMID:15123433 doi:10.1016/j.jmb.2004.03.049
- ↑ 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
- ↑ 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
