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[[Image:1suv.jpg|left|200px]]<br /><applet load="1suv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1suv" />
'''Structure of Human Transferrin Receptor-Transferrin Complex'''<br />


==Overview==
==Structure of Human Transferrin Receptor-Transferrin Complex==
Iron, insoluble as free Fe(3+) and toxic as free Fe(2+), is distributed through the body as Fe(3+) bound to transferrin (Tf) for delivery to cells by endocytosis of its complex with transferrin receptor (TfR). Although much is understood of the transferrin endocytotic cycle, little has been uncovered of the molecular details underlying the formation of the receptor-transferrin complex. Using cryo-electron microscopy, we have produced a density map of the TfR-Tf complex at subnanometer resolution. An atomic model, obtained by fitting crystal structures of diferric Tf and the receptor ectodomain into the map, shows that the Tf N-lobe is sandwiched between the membrane and the TfR ectodomain and that the C-lobe abuts the receptor helical domain. When Tf binds receptor, its N-lobe moves by about 9 A with respect to its C-lobe. The structure of TfR-Tf complex helps account for known differences in the iron-release properties of free and receptor bound Tf.
<SX load='1suv' size='340' side='right' viewer='molstar' caption='[[1suv]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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>
== 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/su/1suv_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=1suv ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
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]]
*[[Transferrin 3D structures|Transferrin 3D structures]]
 
*[[Transferrin receptor|Transferrin receptor]]
==About this Structure==
== References ==
1SUV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1SUV OCA].
<references/>
 
__TOC__
==Reference==
</SX>
Structure of the human transferrin receptor-transferrin complex., Cheng Y, Zak O, Aisen P, Harrison SC, Walz T, Cell. 2004 Feb 20;116(4):565-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14980223 14980223]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Aisen, P.]]
[[Category: Aisen P]]
[[Category: Cheng, Y.]]
[[Category: Cheng Y]]
[[Category: Harrison, S C.]]
[[Category: Harrison SC]]
[[Category: Walz, T.]]
[[Category: Walz T]]
[[Category: Zak, O.]]
[[Category: Zak O]]
[[Category: CO3]]
[[Category: FE]]
[[Category: protein complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:24 2008''

Latest revision as of 11:35, 1 May 2024

Structure of Human Transferrin Receptor-Transferrin ComplexStructure of Human Transferrin Receptor-Transferrin Complex

1suv, resolution 7.50Å

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