1suv

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{{STRUCTURE_1suv| PDB=1suv | SCENE= }}
 
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===Structure of Human Transferrin Receptor-Transferrin Complex===
 
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{{ABSTRACT_PUBMED_14980223}}
 
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==Disease==
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==Structure of Human Transferrin Receptor-Transferrin Complex==
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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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<SX load='1suv' size='340' side='right' viewer='molstar' caption='[[1suv]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[1suv]] is a 6 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=1SUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUV FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/TFR1_HUMAN TFR1_HUMAN]] Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site.<ref>PMID:3568132</ref> [[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.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.5&#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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==About this Structure==
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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=1suv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suv OCA], [https://pdbe.org/1suv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1suv RCSB], [https://www.ebi.ac.uk/pdbsum/1suv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1suv ProSAT]</span></td></tr>
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[[1suv]] is a 6 chain structure with 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=1SUV OCA].
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TFR1_HUMAN TFR1_HUMAN] Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site.<ref>PMID:3568132</ref>
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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/su/1suv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1suv ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Transferrin|Transferrin]]
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*[[Transferrin 3D structures|Transferrin 3D structures]]
*[[Transferrin receptor|Transferrin receptor]]
*[[Transferrin receptor|Transferrin receptor]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:014980223</ref><references group="xtra"/><references/>
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__TOC__
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</SX>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Aisen, P.]]
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[[Category: Large Structures]]
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[[Category: Cheng, Y.]]
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[[Category: Aisen P]]
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[[Category: Harrison, S C.]]
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[[Category: Cheng Y]]
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[[Category: Walz, T.]]
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[[Category: Harrison SC]]
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[[Category: Zak, O.]]
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[[Category: Walz T]]
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[[Category: Metal transport]]
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[[Category: Zak O]]
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[[Category: Protein complex]]
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Current revision

Structure of Human Transferrin Receptor-Transferrin Complex

1suv, resolution 7.50Å

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