1a8e

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[[Image:1a8e.png|left|200px]]
 
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{{STRUCTURE_1a8e| PDB=1a8e | SCENE= }}
{{STRUCTURE_1a8e| PDB=1a8e | SCENE= }}
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===HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE===
===HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE===
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{{ABSTRACT_PUBMED_9609685}}
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{{ABSTRACT_PUBMED_9609685}}
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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:009609685</ref><ref group="xtra">PMID:011917145</ref><references group="xtra"/>
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<ref group="xtra">PMID:009609685</ref><ref group="xtra">PMID:011917145</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Anderson, B F.]]
[[Category: Anderson, B F.]]

Revision as of 10:56, 24 March 2013

Template:STRUCTURE 1a8e

Contents

HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE

Template:ABSTRACT PUBMED 9609685

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

1a8e is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, Bewley M, Smith CA, Murphy ME, Wang Y, Mason AB, Woodworth RC, Brayer GD, Baker EN. Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release. Biochemistry. 1998 Jun 2;37(22):7919-28. PMID:9609685 doi:10.1021/bi980355j
  • Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145
  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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