1oqh

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[[Image:1oqh.png|left|200px]]
 
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{{STRUCTURE_1oqh| PDB=1oqh | SCENE= }}
{{STRUCTURE_1oqh| PDB=1oqh | SCENE= }}
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===Crystal Structure of the R124A mutant of the N-lobe human transferrin===
===Crystal Structure of the R124A mutant of the N-lobe human transferrin===
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{{ABSTRACT_PUBMED_12795604}}
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{{ABSTRACT_PUBMED_12795604}}
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==Disease==
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[[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==
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[[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==
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<ref group="xtra">PMID:012795604</ref><references group="xtra"/>
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<ref group="xtra">PMID:012795604</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Baker, E N.]]
[[Category: Baker, E N.]]

Revision as of 05:42, 25 March 2013

Template:STRUCTURE 1oqh

Contents

Crystal Structure of the R124A mutant of the N-lobe human transferrin

Template:ABSTRACT PUBMED 12795604

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

1oqh is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Baker HM, He QY, Briggs SK, Mason AB, Baker EN. Structural and functional consequences of binding site mutations in transferrin: crystal structures of the Asp63Glu and Arg124Ala mutants of the N-lobe of human transferrin. Biochemistry. 2003 Jun 17;42(23):7084-9. PMID:12795604 doi:http://dx.doi.org/10.1021/bi020689f
  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

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