User:John Hangasky/Sandbox 1 - Revision history

John Hangasky at 19:46, 3 February 2013

John Hangasky — Sun, 03 Feb 2013 19:46:41 GMT

←Older revision		Revision as of 19:46, 3 February 2013
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	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/6'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. The coordination of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'>active site ligands</scene> are seen here. The sixth coordination site is usually occupied by water, not shown here. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.		The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/6'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. The coordination of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'>active site ligands</scene> are seen here. The sixth coordination site is usually occupied by water, not shown here. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.
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-	=== Enzyme Surface ===
-
-	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.

John Hangasky: /* Active Site */

John Hangasky — Wed, 07 Dec 2011 18:47:02 GMT

Active Site

←Older revision		Revision as of 18:47, 7 December 2011
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	=== Active Site===		=== Active Site===

-	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/5'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. The coordination of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'>active site ligands</scene> are seen here. The sixth coordination site is usually occupied by water, not shown here. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.	+	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/6'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. The coordination of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'>active site ligands</scene> are seen here. The sixth coordination site is usually occupied by water, not shown here. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.

	=== Enzyme Surface ===		=== Enzyme Surface ===

	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.		In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.

John Hangasky: /* Active Site */

John Hangasky — Wed, 07 Dec 2011 18:44:33 GMT

Active Site

←Older revision		Revision as of 18:44, 7 December 2011
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	=== Active Site===		=== Active Site===

-	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. The coordination of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'>active site ligands</scene> are seen here. The sixth coordination site is usually occupied by water, not shown here. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.	+	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/5'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. The coordination of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'>active site ligands</scene> are seen here. The sixth coordination site is usually occupied by water, not shown here. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.

	=== Enzyme Surface ===		=== Enzyme Surface ===

	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.		In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.

John Hangasky: /* Active Site */

John Hangasky — Wed, 07 Dec 2011 18:42:09 GMT

Active Site

←Older revision		Revision as of 18:42, 7 December 2011
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	=== Active Site===		=== Active Site===

-	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. ~~In the depiction~~ of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>~~FIH Active Site Ligands~~</scene> ~~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. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.	+	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. The coordination of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'>active site ligands</scene> are seen here. The sixth coordination site is usually occupied by water, not shown here. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.

	=== Enzyme Surface ===		=== Enzyme Surface ===

	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.		In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.

John Hangasky: /* Active Site */

John Hangasky — Wed, 07 Dec 2011 17:29:35 GMT

Active Site

←Older revision		Revision as of 17:29, 7 December 2011
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	=== Active Site===		=== Active Site===

-	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. In the depiction of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene> 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.	+	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. In the depiction of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene> 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. Upon binding of substrate, it is believed this water is released and the iron becomes five coordinate.

	=== Enzyme Surface ===		=== Enzyme Surface ===

	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.		In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.

John Hangasky: /* Enzyme Surface */

John Hangasky — Fri, 30 Apr 2010 18:55:51 GMT

Enzyme Surface

←Older revision		Revision as of 18:55, 30 April 2010
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	=== Enzyme Surface ===		=== Enzyme Surface ===

-	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is ~~seen~~.	+	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is shown.

John Hangasky: /* Active Site */

John Hangasky — Fri, 30 Apr 2010 18:55:30 GMT

Active Site

←Older revision		Revision as of 18:55, 30 April 2010
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	=== Active Site===		=== Active Site===

-	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> 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 <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene> 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.	+	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> contains an Iron (II) core. The Iron core is coordinated by 2 histidine residues, an aspartate residue, an α-ketoglutarate molecule, and one water molecule. The Iron (II) is six coordinated, with α-KG chelating in a bidentate manner. In the depiction of the <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene> 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 ===		=== Enzyme Surface ===

	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is seen.		In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is seen.

John Hangasky: /* Factor Inhibiting HIF */

John Hangasky — Fri, 30 Apr 2010 18:51:10 GMT

Factor Inhibiting HIF

←Older revision		Revision as of 18:51, 30 April 2010
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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 ~~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.	+	'''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 ~~activation domain~~ (CTAD) of HIF. This binding domain, <scene name='User:John_Hangasky/Sandbox_1/Fih/5'>CTAD</scene>, colored teal.	+	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===

John Hangasky at 18:26, 30 April 2010

John Hangasky — Fri, 30 Apr 2010 18:26:18 GMT

←Older revision		Revision as of 18:26, 30 April 2010
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	The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> 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 <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene> 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.		The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> 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 <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene> 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.
-
-	<scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'>FIH Active Site Ligands</scene>

	=== Enzyme Surface ===		=== Enzyme Surface ===

	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is seen.		In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is seen.

John Hangasky at 18:24, 30 April 2010

John Hangasky — Fri, 30 Apr 2010 18:24:33 GMT

←Older revision		Revision as of 18:24, 30 April 2010
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	=== Enzyme Surface ===		=== 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~~.	+	In this depiction, the <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> of FIH is seen.