Transferrin receptor

spinqualitylabelsall models Human transferrin receptor ectodomain dimer (grey and green) complex with transferrin N-lobe (pink and yellow) and C-lobe (cyan and magenta) and carbonate, 1suv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Transferrin receptor (TfR) imports iron into the cell by receptor-mediated endocytosis of transferrin-iron complex. TfR is regulated by intracellular iron concentration. The amount of TfR expressed on the cell is proportional to the cell’s need for iron. The TfR has selective affinity for diferric-transferrin. The TfR-transferrin complex is internalized by the cell and iron is released to the cytosol. The TfR-apotransferrin complex returns to the extracellular surface where the apotransferrin dissociates and is replaced by diferric-transferrin. Relevance TfR is a potential determinant of iron loading in congenital anemias. Structural highlights Human transferrin receptor ectodomain dimer complex with transferrin N-lobe and C-lobe (1suv).

3D structures of transferrin receptor

transferrin – hTfR ectodomain – human
1suv - hTfR ectodomain + hemochromatosis protein + β-2-microglobulin
1suv - hTfR ectodomain + transferrin
3s9l, 3s9m, 3s9n - hTfR ectodomain + transferrin N-lobe
2nsu - hTfR ectodomain in dog retrovirus – Cryo EM
3kas - hTfR ectodomain + Machupo virus GP1

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Michal Harel, Alexander Berchansky, Joel L. Sussman