User:Khaja Muneeruddin/Sandbox 1
From Proteopedia
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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. | ||
| - | <scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotransferrin/2'>Human Transferrin</scene>is a 80 KDa bilobal glycoprotein. The N-lobe and C-lobe of hTf binds to one ferric ion each to keep ferric ion in solution or transport to iron requiring cells. | + | <scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotransferrin/2'>Human Transferrin</scene> is a 80 KDa bilobal glycoprotein. The N-lobe and C-lobe of hTf binds to one ferric ion each to keep ferric ion in solution or transport to iron requiring cells. |
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. | 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. | ||
Revision as of 16:22, 8 December 2011
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is a 80 KDa bilobal glycoprotein. The N-lobe and C-lobe of hTf binds to one ferric ion each to keep ferric ion in solution or transport to iron requiring cells.
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.
