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 glycoprotein. In Apo transferrin, 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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<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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Diferric HTf binds to human transferrin receptor (hTfR) expressed on the surface of iron requiring cells. Upon binding, Fe2hTf-hTfR is internalized in the cell by endocytosis. The acidic condition of endosome causes the release of ferric ions in cells and the ApohTf-HTfR is recycled back to cell surface to release ApohTf in plasma where it can bind to ferric ions again.
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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

Revision as of 23:17, 12 December 2011

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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

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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Khaja Muneeruddin

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