View source for 11rn


==Complex of B19V VP1u RBD and human transferrin receptor ectodomain==
<StructureSection load='11rn' size='340' side='right'caption='[[11rn]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[11rn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_parvovirus_B19 Human parvovirus B19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=11RN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=11RN 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=11rn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=11rn OCA], [https://pdbe.org/11rn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=11rn RCSB], [https://www.ebi.ac.uk/pdbsum/11rn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=11rn 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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human parvovirus B19]]
[[Category: Large Structures]]
[[Category: Hafenstein S]]
[[Category: Lee H]]
[[Category: Ros C]]