User:John Hangasky/Sandbox 1
From Proteopedia
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The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> contains an 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. | The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> contains an 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. | ||
| - | <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'> | + | <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene> |
=== Oxygen Channel === | === Oxygen Channel === | ||
For FIH to modify its substrate, molecular oxygen must reach the active site. Since the active site is buried within the enzyme, oxygen must reach the active site via an oxygen channel. An <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'>Oxygen Channel</scene> has been proposed, leading to this active site. | For FIH to modify its substrate, molecular oxygen must reach the active site. Since the active site is buried within the enzyme, oxygen must reach the active site via an oxygen channel. An <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'>Oxygen Channel</scene> has been proposed, leading to this active site. | ||
Revision as of 17:48, 30 April 2010
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| 1h2l, resolution 2.25Å () | |||||||||
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| Ligands: | , , | ||||||||
| Related: | 1d7g, 1h2k, 1h2m, 1h2n, 1l8c, 1lm8, 1lqb | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Factor Inhibiting HIF
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.
Active Site
The contains an 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.
Oxygen Channel
For FIH to modify its substrate, molecular oxygen must reach the active site. Since the active site is buried within the enzyme, oxygen must reach the active site via an oxygen channel. An has been proposed, leading to this active site.
