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[[Image:1d3k.jpg|left|200px]]


{{Structure
==HUMAN SERUM TRANSFERRIN==
|PDB= 1d3k |SIZE=350|CAPTION= <scene name='initialview01'>1d3k</scene>, resolution 1.8&Aring;
<StructureSection load='1d3k' size='340' side='right'caption='[[1d3k]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>
<table><tr><td colspan='2'>[[1d3k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D3K FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3k OCA], [https://pdbe.org/1d3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d3k RCSB], [https://www.ebi.ac.uk/pdbsum/1d3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d3k ProSAT]</span></td></tr>
|RELATEDENTRY=[[1a8e|1A8E]], [[1a8f|1A8F]], [[1d4n|1D4N]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3k OCA], [http://www.ebi.ac.uk/pdbsum/1d3k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d3k RCSB]</span>
== Disease ==
}}
[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[https://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 ==
[https://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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d3/1d3k_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d3k ConSurf].
<div style="clear:both"></div>


'''HUMAN SERUM TRANSFERRIN'''
==See Also==
 
*[[Transferrin 3D structures|Transferrin 3D structures]]
 
== References ==
==Overview==
<references/>
The X-ray crystallographic structures of two mutants (K206Q and H207E) of the N-lobe of human transferrin (hTF/2N) have been determined to high resolution (1.8 and 2.0 A, respectively). Both mutant proteins bind iron with greater affinity than native hTF/2N. The structures of the K206Q and H207E mutants show interactions (both H-bonding and electrostatic) that stabilize the interaction of Lys296 in the closed conformation, thereby stabilizing the iron bound forms.
__TOC__
 
</StructureSection>
==About this Structure==
1D3K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D3K OCA].
 
==Reference==
Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron., Yang AH, MacGillivray RT, Chen J, Luo Y, Wang Y, Brayer GD, Mason AB, Woodworth RC, Murphy ME, Protein Sci. 2000 Jan;9(1):49-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10739246 10739246]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brayer, G D.]]
[[Category: Brayer GD]]
[[Category: Chen, J.]]
[[Category: Chen J]]
[[Category: Luo, Y.]]
[[Category: Luo Y]]
[[Category: MacGillivray, R T.A.]]
[[Category: MacGillivray RTA]]
[[Category: Mason, A.]]
[[Category: Mason A]]
[[Category: Murphy, M E.P.]]
[[Category: Murphy MEP]]
[[Category: Wang, Y.]]
[[Category: Wang Y]]
[[Category: Woodworth, R C.]]
[[Category: Woodworth RC]]
[[Category: Yang, H W.]]
[[Category: Yang H-W]]
[[Category: carbonate]]
[[Category: glycoprotein]]
[[Category: iron transport]]
[[Category: iron-release]]
[[Category: nlobe]]
[[Category: transferrin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:33:57 2008''

Latest revision as of 18:45, 13 March 2024

HUMAN SERUM TRANSFERRINHUMAN SERUM TRANSFERRIN

Structural highlights

1d3k is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  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

1d3k, resolution 1.80Å

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