User:Khaja Muneeruddin/Sandbox 1

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One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

is a 80 KDa bilobal, iron binding glycoprotein. In Apo transferrin (iron free form), N-lobe (brown) and C-lobe (green) bind to one ferric ion each to keep ferric ion in solution or transport to iron requiring cells

Both at the N-lobe and C-lobe specific amino acid residues are involved in binding to ferric ion. At the binding site of C-lobe so and so residues are involved in trapping iron. The amino acids involved in trapping of iron at the bind site of N-lobe includes. N lobe and C lobe undergoes a large conformational change upon binding to ferric ion. Open N-lobe characteristics and upon binding to iron closed N lobe looks like this.

Transferrin delivers iron to iron requiring cells by receptor-mediated endocytosis. At basic pH of cell surface diferric HTf binds to human transferrin receptor (hTfR). Upon binding, iron bound hTf-hTfR is internalized in the cell by endocytosis. In the acidic condition of endosome iron is release from hTf into the cells. The ApohTf-HTfR complex is recycled back to the cell surface and at the basic pH of cell surface transferrin unbounds from the TfR^[1]. Both N-lobe and C-lobe undergoes

show each binding site and label residues.

References

1. ↑ Giannetti AM, Halbrooks PJ, Mason AB, Vogt TM, Enns CA, Bjorkman PJ. The molecular mechanism for receptor-stimulated iron release from the plasma iron transport protein transferrin. Structure. 2005 Nov;13(11):1613-23. PMID:16271884 doi:10.1016/j.str.2005.07.016