User:John Hangasky/Sandbox 1
From Proteopedia
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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. In normoxic conditions, molecular oxygen is used to hydroxylate HIF, preventing HIF to bind to p300. However, in hypoxic environments, 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. An <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'>Oxygen Channel</scene> has been proposed, and studies are under way, testing this proposed channel. | 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. In normoxic conditions, molecular oxygen is used to hydroxylate HIF, preventing HIF to bind to p300. However, in hypoxic environments, 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. An <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'>Oxygen Channel</scene> has been proposed, and studies are under way, testing this proposed channel. | ||
Revision as of 20:12, 28 April 2010
Factor inhibiting HIF is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body. In normoxic conditions, molecular oxygen is used to hydroxylate HIF, preventing HIF to bind to p300. However, in hypoxic environments, this hydroxylation does not occur. For this sensing to occur, molecular oxygen must reach the at the iron core. An has been proposed, and studies are under way, testing this proposed channel.
