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User:Khaja Muneeruddin/Sandbox 1
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<Structure load='2HAU' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />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. | <Structure load='2HAU' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />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. | ||
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<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apo_transferrin/5'>Human Transferrin (hTf)</scene> 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 | <scene name='User:Khaja_Muneeruddin/Sandbox_1/Apo_transferrin/5'>Human Transferrin (hTf)</scene> 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 | ||
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| + | 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. | ||
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. Both N-lobe and C-lobe undergoes | 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. Both N-lobe and C-lobe undergoes | ||
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| + | show each binding site and label residues. | ||
Revision as of 03:43, 14 December 2011
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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.
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. Both N-lobe and C-lobe undergoes
show each binding site and label residues.
