Iron, insoluble as free Fe3+ and toxic as free Fe2+, is distributed through the body as Fe3+ bound to transferrin (Tf) for delivery to cells by endocytosis of its complex with transferrin receptor (TfR). Endosomal acidification leads to iron release. The receptor-binding domain of the Machupo virus GP1 protein (purple) is shown bound to the TfR1 apical domain. Rapidly proliferating cells have higher iron requirements 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). Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. The structure of a transferrin receptor from the parasite Trypanosoma brucei in complex with human transferrin helps to understand how the parasite can use surface exposed receptors to … - sTfR complex.

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. Transferrin has two homologous globular lobes, the N- and C- terminals comprised of alpha helices and beta sheets, with an iron binding site in between.

The image above is a 3-D depiction of human transferrin protein. The RCSB PDB also provides a variety of tools and resources. 2004 Feb 20;116(4):483-5. The property as well as geometry of the derived complex was also presented. Iron, insoluble as free Fe3+ and toxic as free Fe2+, is distributed through the body as Fe3+ bound to transferrin (Tf) for delivery to cells by endocytosis of its complex with transferrin receptor (TfR). The existence of a receptor for transferrin iron uptake had been recognized over half a century back. 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. transferrin, the serum iron transport protein, to the transferrin receptor, followed by the internalization of the receptor-transferrin complex. Structurally speaking, Transferrin is a polypeptide chain consisting of two carbohydrate chains and almost seven hundred amino acids. Comment in Cell.

The receptor has been identified as a proliferation specific marker. Structure of the human transferrin receptor-transferrin complex. 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. 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.

After binding to the transferrin receptor and being brought into the cell by endocytosis, the transferrin molecule is stimulated by a pH reduction in the endosome to release its iron ligands, forming the iron-free transferrin-receptor-transferrin complex (no crystal structure is available for this structure) (4).

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