1d4n

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[[Image:1d4n.jpg|left|200px]]<br /><applet load="1d4n" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d4n, resolution 2.00&Aring;" />
 
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'''HUMAN SERUM TRANSFERRIN'''<br />
 
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==Overview==
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==HUMAN SERUM TRANSFERRIN==
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<StructureSection load='1d4n' size='340' side='right'caption='[[1d4n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d4n]] 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=1D4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D4N FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4n OCA], [https://pdbe.org/1d4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d4n RCSB], [https://www.ebi.ac.uk/pdbsum/1d4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d4n ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d4/1d4n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1d4n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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.
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==Disease==
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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:10739246<ref>PMID:10739246</ref>
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Known diseases associated with this structure: Atransferrinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190000 190000]], Iron deficiency anemia, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190000 190000]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1D4N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CO3:'>CO3</scene> and <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4N OCA].
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</div>
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<div class="pdbe-citations 1d4n" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10739246 10739246]
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*[[Transferrin 3D structures|Transferrin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brayer, G D.]]
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[[Category: Brayer GD]]
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[[Category: Chen, J.]]
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[[Category: Chen J]]
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[[Category: Luo, Y.]]
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[[Category: Luo Y]]
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[[Category: MacGillivray, R T.A.]]
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[[Category: MacGillivray RTA]]
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[[Category: Mason, A.]]
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[[Category: Mason A]]
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[[Category: Murphy, M E.P.]]
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[[Category: Murphy MEP]]
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[[Category: Wang, Y.]]
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[[Category: Wang Y]]
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[[Category: Woodworth, R C.]]
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[[Category: Woodworth RC]]
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[[Category: Yang, H W.]]
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[[Category: Yang H-W]]
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[[Category: CO3]]
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[[Category: FE]]
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[[Category: carbonate]]
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[[Category: glycoprotein]]
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[[Category: iron transport]]
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[[Category: iron-release]]
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[[Category: n-lobe]]
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[[Category: transferrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:56 2008''
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Current revision

HUMAN SERUM TRANSFERRIN

PDB ID 1d4n

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