2o7u
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_2o7u| PDB=2o7u | SCENE= }} | {{STRUCTURE_2o7u| PDB=2o7u | SCENE= }} | ||
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===Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin=== | ===Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin=== | ||
+ | {{ABSTRACT_PUBMED_17327678}} | ||
- | + | ==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:017327678</ref><references group="xtra"/> | + | <ref group="xtra">PMID:017327678</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Baker, E N.]] | [[Category: Baker, E N.]] |
Revision as of 07:01, 25 March 2013
Contents |
Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin
Template:ABSTRACT PUBMED 17327678
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
2o7u is a 9 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Baker HM, Nurizzo D, Mason AB, Baker EN. Structures of two mutants that probe the role in iron release of the dilysine pair in the N-lobe of human transferrin. Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):408-14. Epub 2007, Feb 21. PMID:17327678 doi:10.1107/S0907444907000182
- ↑ 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