1cx8

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cx8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cx8 RCSB], [http://www.ebi.ac.uk/pdbsum/1cx8 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cx8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cx8 RCSB], [http://www.ebi.ac.uk/pdbsum/1cx8 PDBsum]</span></td></tr>
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== Function ==
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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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 12:04, 25 December 2014

CRYTAL STRUCTURE OF THE ECTODOMAIN OF HUMAN TRANSFERRIN RECEPTOR

1cx8, resolution 3.20Å

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