User:John Hangasky/Sandbox 1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 13: Line 13:
<scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene>
<scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene>
-
=== Oxygen Channel ===
+
=== Enzyme Surface ===
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 18:14, 30 April 2010

PDB ID 1h2l

Drag the structure with the mouse to rotate
1h2l, resolution 2.25Å ()
Ligands: , ,
Related: 1d7g, 1h2k, 1h2m, 1h2n, 1l8c, 1lm8, 1lqb
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.

FIH binds to the C-terminal activation domain (CTAD) of HIF. This binding domain, , colored teal.

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

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.

Proteopedia Page Contributors and Editors (what is this?)

John Hangasky

Personal tools