User:John Hangasky/Sandbox 1
From Proteopedia
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In normoxic conditions (high oxygen concenrations), molecular oxygen is used to hydroxylate HIF, preventing HIF from binding to p300, a transcription coactivator. However, in hypoxic conditions (low oxygen concentrations), this hydroxylation does not occur. | In normoxic conditions (high oxygen concenrations), molecular oxygen is used to hydroxylate HIF, preventing HIF from binding to p300, a transcription coactivator. However, in hypoxic conditions (low oxygen concentrations), this hydroxylation does not occur. | ||
| - | For this sensing to occur, molecular oxygen must reach the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'>FIH active site</scene> at the iron core. The iron core is coordinated by 2 histidine residues, an asparagine residue, α-ketoglutarate and one water molecule. α-ketoglutarate chelates in a bidentate manner, making the coordination number of the iron 6. An <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'>Oxygen Channel</scene> has been proposed, | + | For this sensing to occur, molecular oxygen must reach the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'>FIH active site</scene> at the iron core. The iron core is coordinated by 2 histidine residues, an asparagine residue, α-ketoglutarate and one water molecule. α-ketoglutarate chelates in a bidentate manner, making the coordination number of the iron 6. |
| - | + | An <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'>Oxygen Channel</scene> has been proposed, leading to this active site. | |
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Factor inhibiting HIF <scene name='User:John_Hangasky/Sandbox_1/Fih/2'>(FIH)</scene> is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body. | Factor inhibiting HIF <scene name='User:John_Hangasky/Sandbox_1/Fih/2'>(FIH)</scene> is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body. | ||
Revision as of 21:35, 28 April 2010
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Hypoxia Inducible Factor (HIF)is a transcription activator that regulates over 100 genes, many of which are important for development. HIF has been found to be over expressed in many cancers. Factor Inhibing HIF (FIH) is a non-heme Iron (II) α-ketoglutarate dependent asparaginyl hydroxylase that regulates HIF.
In normoxic conditions (high oxygen concenrations), molecular oxygen is used to hydroxylate HIF, preventing HIF from binding to p300, a transcription coactivator. However, in hypoxic conditions (low oxygen concentrations), this hydroxylation does not occur.
For this sensing to occur, molecular oxygen must reach the at the iron core. The iron core is coordinated by 2 histidine residues, an asparagine residue, α-ketoglutarate and one water molecule. α-ketoglutarate chelates in a bidentate manner, making the coordination number of the iron 6.
An has been proposed, leading to this active site.
Factor inhibiting HIF is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body.
