User:John Hangasky/Sandbox 1
From Proteopedia
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=== Factor Inhibiting HIF === | === Factor Inhibiting HIF === | ||
| - | '''H'''ypoxia '''I'''nducible '''F'''actor (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. '''F'''actor '''I'''nhibing '''H'''IF (FIH) is a non-heme Iron (II) α-ketoglutarate dependent asparaginyl hydroxylase that regulates HIF. In normoxic conditions (high oxygen | + | '''H'''ypoxia '''I'''nducible '''F'''actor (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. '''F'''actor '''I'''nhibing '''H'''IF (FIH) is a non-heme Iron (II) α-ketoglutarate (α-KG) dependent asparaginyl hydroxylase that regulates HIF. In normoxic conditions (high oxygen concentrations), molecular oxygen is used to hydroxylate HIF, preventing HIF from binding to p300, a transcription co-activator. However, in hypoxic conditions (low oxygen concentrations), this hydroxylation does not occur. |
| - | FIH binds to the C-terminal | + | FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, <scene name='User:John_Hangasky/Sandbox_1/Fih/5'>CTAD</scene>, is colored teal in this depiction. |
=== Active Site=== | === Active Site=== | ||
Revision as of 18:51, 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 (α-KG) dependent asparaginyl hydroxylase that regulates HIF. In normoxic conditions (high oxygen concentrations), molecular oxygen is used to hydroxylate HIF, preventing HIF from binding to p300, a transcription co-activator. However, in hypoxic conditions (low oxygen concentrations), this hydroxylation does not occur.
FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, , is colored teal in this depiction.
Active Site
The contains an iron II 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. In the depiction of the Histidines are colored blue, Aspartate is colored red, Iron is the white sphere, and α-KG is colored yellow. The sixth coordination site is usually occupied by water, not shown here.
Enzyme Surface
In this depiction, the of FIH is seen.
