User:John Hangasky/Sandbox 1

From Proteopedia

spinqualitylabelsall models PDB ID 1h2l Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1h2l, resolution 2.25Å ()
Ligands:	, ,
Related:	1d7g, 1h2k, 1h2m, 1h2n, 1l8c, 1lm8, 1lqb
Structural annotation: Resources: InterPro : Ipr003347, Ipr013109, Ipr001321, Ipr001610, Ipr013655, Ipr013767, Ipr014887, Ipr001092, Ipr000014, Ipr011598 Pfam : PF08007, PF08778 SCOP : d1h2la_, d1h2ls_ UniProt : Q9NWT6, Q16665
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

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.