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| | <StructureSection load='1cx8' size='340' side='right'caption='[[1cx8]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='1cx8' size='340' side='right'caption='[[1cx8]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1cx8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. The November 2002 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Ferritin and Transferrin'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2002_11 10.2210/rcsb_pdb/mom_2002_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1cx8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. The November 2002 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Ferritin and Transferrin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2002_11 10.2210/rcsb_pdb/mom_2002_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CX8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene></td></tr> | + | </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>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene></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://pdbe.org/1cx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cx8 RCSB], [http://www.ebi.ac.uk/pdbsum/1cx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cx8 ProSAT]</span></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=1cx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cx8 OCA], [https://pdbe.org/1cx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cx8 RCSB], [https://www.ebi.ac.uk/pdbsum/1cx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cx8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [[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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Human Hemochromatosis Protein|Human Hemochromatosis Protein]] | + | *[[Hemochromatosis protein|Hemochromatosis protein]] |
| | *[[Transferrin receptor|Transferrin receptor]] | | *[[Transferrin receptor|Transferrin receptor]] |
| | == References == | | == References == |
| Structural highlights
Function
[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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome. The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit. One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure. A model is proposed for Tf binding to the receptor.
Crystal structure of the ectodomain of human transferrin receptor.,Lawrence CM, Ray S, Babyonyshev M, Galluser R, Borhani DW, Harrison SC Science. 1999 Oct 22;286(5440):779-82. PMID:10531064[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rothenberger S, Iacopetta BJ, Kuhn LC. Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site. Cell. 1987 May 8;49(3):423-31. PMID:3568132
- ↑ Lawrence CM, Ray S, Babyonyshev M, Galluser R, Borhani DW, Harrison SC. Crystal structure of the ectodomain of human transferrin receptor. Science. 1999 Oct 22;286(5440):779-82. PMID:10531064
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