Proteopedia - User contributions [en]

User:Cornelius Taabazuing/sandbox 1

2011-12-07T18:19:35Z

Cornelius Taabazuing:

{{STRUCTURE_1h2l| PDB=1h2l | SIZE=300| SCENE=User:John_Hangasky/Sandbox_1/Fih/4|right| CAPTION=Human HIF complex with Fe+2, sulfate and alpha ketogluterate, [[1h2l]] }}

=== Factor Inhibiting HIF ===

'''H'''ypoxia '''I'''nducible '''F'''actor (HIF)is a heterodimeric transcription factor that regulates over 100 genes. HIF consists of a constitutively expressed beta subunit, and an alpha subunit that is regulated in oxygen dependent manor. There are two enzymes that regulate HIF controlled gene expression, '''F'''actor '''I'''nhibiting '''H'''IF (FIH) and '''P'''rolyl '''H'''ydroxylase '''D'''omain 2 (PHD2). During normoxic conditions, Hydroxylation of one of two or both proline residues in the Oxygen Degradation Domain (ODD) of HIF results in proteosomal degradation of the HIF alpha subunit. Hydroxylation of an asparagine residue in the C-terminal Trans-Activation Domain (<scene name='User:John_Hangasky/Sandbox_1/Fih/5'>CTAD</scene>) of HIF by FIH results in transcriptional silencing of genes due to HIF's inability to recruit the co-activator p300. However, under hypoxic conditions, there is no hydroxylation, resulting in stabilization of the HIF alpha subunit. The alpha subunit dimerizes with the beta subunit and HIF is able to transcribe genes important for red blood cell production, metabolic activity, angiogenesis,development, and many other functions.

=== Active Site===

The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> (CT)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> (BH) 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 <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> (JH) of FIH is shown.

===3D structures of HIF===

[[Hypoxia-inducible factor]]

==Additional Resources==
For additional information, see: [[Cancer]]
<br />

User:Cornelius Taabazuing/sandbox 1

2011-12-07T18:15:56Z

Cornelius Taabazuing:

{{STRUCTURE_1h2l| PDB=1h2l | SIZE=300| SCENE=User:John_Hangasky/Sandbox_1/Fih/4|right| CAPTION=Human HIF complex with Fe+2, sulfate and alpha ketogluterate, [[1h2l]] }}

=== Factor Inhibiting HIF ===

'''H'''ypoxia '''I'''nducible '''F'''actor (HIF)is a heterodimeric transcription factor that regulates over 100 genes. HIF consists of a constitutively expressed beta subunit, and an alpha subunit that is regulated in oxygen dependent manor. There are two enzymes that regulate HIF controlled gene expression, '''F'''actor '''I'''nhibiting '''H'''IF (FIH) and '''P'''rolyl '''H'''ydroxylase '''D'''omain 2 (PHD2). During normoxic conditions, Hydroxylation of one of two or both proline residues in the Oxygen Degradation Domain (ODD) of HIF results in proteosomal degradation of the HIF alpha subunit. Hydroxylation of an asparagine residue in the C-terminal Trans-Activation Domain (CTAD) of HIF by FIH results in transcriptional silencing of genes due to HIF's inability to recruit the co-activator p300. However, under hypoxic conditions, there is no hydroxylation, resulting in stabilization of the HIF alpha subunit. The alpha subunit dimerizes with the beta subunit and HIF is able to transcribe genes important for red blood cell production, metabolic activity, angiogenesis,development, and many other functions.

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>, (JH)is colored teal in this depiction.

=== Active Site===

The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> (CT)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> (BH) 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 <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> (JH) of FIH is shown.

===3D structures of HIF===

[[Hypoxia-inducible factor]]

==Additional Resources==
For additional information, see: [[Cancer]]
<br />

Molecular Playground/FIH

2011-12-07T18:07:28Z

Cornelius Taabazuing:

{{STRUCTURE_1h2l| PDB=1h2l | SIZE=300| SCENE=User:John_Hangasky/Sandbox_1/Fih/4|right| CAPTION=Human HIF complex with Fe+2, sulfate and 2-oxoglutaric acid, [[1h2l]] }}

=== Factor Inhibiting HIF ===

'''H'''ypoxia '''I'''nducible '''F'''actor (HIF)is a heterodimeric transcription factor that regulates over 100 genes. HIF consists of a constitutively expressed beta subunit, and an alpha subunit that is regulated in oxygen dependent manor. There are two enzymes that regulate HIF controlled gene expression, '''F'''actor '''I'''nhibiting '''H'''IF (FIH) and '''P'''rolyl '''H'''ydroxylase '''D'''omain 2 (PHD2). During normoxic conditions, Hydroxylation of one of two or both proline residues in the Oxygen Degradation Domain (ODD) of HIF results in proteosomal degradation of the HIF alpha subunit. Hydroxylation of an asparagine residue in the C-Terminal Trans-Activation Domain (CTAD) of HIF by FIH results in transcriptional silencing of genes due to HIF's inability to recruit the co-activator p300. However, under hypoxic conditions, there is no hydroxylation, resulting in stabilization of the HIF alpha subunit. The alpha subunit dimerizes with the beta subunit and HIF is able to transcribe genes important for red blood cell production, metabolic activity, angiogenesis,development, and many other functions.

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===

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 ===

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

===3D structures of HIF===

[[Hypoxia-inducible factor]]

==Additional Resources==
For additional information, see: [[Cancer]]
<br />

User:Cornelius Taabazuing/sandbox 1

2011-12-07T18:04:44Z

Cornelius Taabazuing: New page: {{STRUCTURE_1h2l| PDB=1h2l | SIZE=300| SCENE=User:John_Hangasky/Sandbox_1/Fih/4|right| CAPTION=Human HIF complex with Fe+2, sulfate and alpha ketogluterate, 1h2l }} === Factor I...

{{STRUCTURE_1h2l| PDB=1h2l | SIZE=300| SCENE=User:John_Hangasky/Sandbox_1/Fih/4|right| CAPTION=Human HIF complex with Fe+2, sulfate and alpha ketogluterate, [[1h2l]] }}

=== Factor Inhibiting HIF ===

'''H'''ypoxia '''I'''nducible '''F'''actor (HIF)is a heterodimeric transcription factor that regulates over 100 genes. HIF consists of a constitutively expressed beta subunit, and an alpha subunit that is regulated in oxygen dependent manor. There are two enzymes that regulate HIF controlled gene expression, '''F'''actor '''I'''nhibiting '''H'''IF (FIH) and '''P'''rolyl '''H'''ydroxylase '''D'''omain 2 (PHD2). During normoxic conditions, Hydroxylation of one of two or both proline residues in the Oxygen Degradation Domain (ODD) of HIF results in proteosomal degradation of the HIF alpha subunit. Hydroxylation of an asparagine residue in the C-Terminal Trans-Activation Domain (CTAD) of HIF by FIH results in transcriptional silencing of genes due to HIF's inability to recruit the co-activator p300. However, under hypoxic conditions, there is no hydroxylation, resulting in stabilization of the HIF alpha subunit. The alpha subunit dimerizes with the beta subunit and HIF is able to transcribe genes important for red blood cell production, metabolic activity, angiogenesis,development, and many other functions.

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>, (JH)is colored teal in this depiction.

=== Active Site===

The <scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'>FIH Active Site</scene> (CT)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> (BH) 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 <scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'>solvent accessible surface</scene> (JH) of FIH is shown.

===3D structures of HIF===

[[Hypoxia-inducible factor]]

==Additional Resources==
For additional information, see: [[Cancer]]
<br />

User:Cornelius Taabazuing/ Sandbox 1

2010-04-27T18:06:42Z

Cornelius Taabazuing:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />

<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/3'>FIH Space Fill</scene>

<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/4'>Scene Skipping Transitions</scene>

User:Cornelius Taabazuing

2010-04-27T04:44:37Z

Cornelius Taabazuing:

My name is Cornelius Taabazuing and I am currently a graduate student in the CBI program at the University of Massachusetts Amherst. I graduated Magna Cum Laude from the University of Massachusetts Amherst and received a Bachelors of Science in Biochemistry and Molecular Biology degree. My current research is focused at developing inhibitors for Factor Inhibiting Hypoxia (FIH), an asparaginyl hydroxylase that regulates Hypoxia Inducible Factor (HIF).

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T15:54:06Z

Cornelius Taabazuing:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />

<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/3'>TextToBeDisplayed</scene>

<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/4'>Scene Skipping Transitions</scene>

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T15:51:13Z

Cornelius Taabazuing:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/1'>TextToBeDisplayed</scene>

<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/2'>TextToBeDisplayed</scene>

<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/3'>TextToBeDisplayed</scene>

<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/4'>Scene Skipping Transitions</scene>

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T15:32:51Z

Cornelius Taabazuing:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/1'>TextToBeDisplayed</scene>
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/2'>TextToBeDisplayed</scene>
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/3'>TextToBeDisplayed</scene>
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/4'>Scene Skipping Transitions</scene>

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T15:28:04Z

Cornelius Taabazuing:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/1'>TextToBeDisplayed</scene>
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/2'>TextToBeDisplayed</scene>
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/3'>TextToBeDisplayed</scene>

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T15:27:03Z

Cornelius Taabazuing:

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T15:20:17Z

Cornelius Taabazuing:

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T15:11:09Z

Cornelius Taabazuing:

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T14:54:36Z

Cornelius Taabazuing:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />
<scene name='User:Cornelius_Taabazuing/_Sandbox_1/Factor_inhibiting_hypoxia/1'>TextToBeDisplayed</scene>

User:Cornelius Taabazuing/ Sandbox 1

2010-03-16T14:34:20Z

Cornelius Taabazuing: New page: <applet size='[450,338]' frame='true' align='right' caption='YYY' />