1n7w
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
==Disease== | ==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> | + | [[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> |
==Function== | ==Function== | ||
| Line 10: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | [[1n7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[1n7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7W OCA]. |
==See Also== | ==See Also== | ||
| Line 17: | Line 17: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:012458193</ref><references group="xtra"/><references/> | <ref group="xtra">PMID:012458193</ref><references group="xtra"/><references/> | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Adams, T E.]] | [[Category: Adams, T E.]] | ||
[[Category: Briggs, S K.]] | [[Category: Briggs, S K.]] | ||
Revision as of 07:34, 16 April 2014
Contents |
Crystal Structure of Human Serum Transferrin, N-Lobe L66W mutant
Template:ABSTRACT PUBMED 12458193
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
1n7w is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA.
See Also
Reference
- Adams TE, Mason AB, He QY, Halbrooks PJ, Briggs SK, Smith VC, MacGillivray RT, Everse SJ. The position of arginine 124 controls the rate of iron release from the N-lobe of human serum transferrin. A structural study. J Biol Chem. 2003 Feb 21;278(8):6027-33. Epub 2002 Nov 27. PMID:12458193 doi:10.1074/jbc.M210349200
- ↑ 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
