https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=John+Hangasky 2026-09-22T15:08:00Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1715502 2013-02-03T19:46:41Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/6'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'&gt;active site ligands&lt;/scene&gt; 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.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_2&diff=1715501 2013-02-03T19:45:49Z

<p>John Hangasky: Removing all content from page</p> <hr /> <div></div>

John Hangasky https://proteopedia.org/index.php?title=Molecular_Playground/FIH&diff=1329718 2011-12-07T18:55:10Z

<p>John Hangasky: </p> <hr /> <div>{{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]] }}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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 (&lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;) 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.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/6'&gt;FIH Active Site&lt;/scene&gt; 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 active site ligands can be seen &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/7'&gt;here&lt;/scene&gt;. The axial coordination position is initially occupied by a water molecule. Upon binding of CTAD, this water molecule is released, opening a coordination site for oxygen to bind.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.<br /> <br /> ===3D structures of HIF===<br /> <br /> [[Hypoxia-inducible factor]]<br /> <br /> ==Additional Resources==<br /> For additional information, see: [[Cancer]]<br /> &lt;br /&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=Molecular_Playground/FIH&diff=1329717 2011-12-07T18:53:22Z

<p>John Hangasky: /* Active Site */</p> <hr /> <div>{{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]] }}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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 (&lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;) 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.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/6'&gt;FIH Active Site&lt;/scene&gt; 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 active site ligands can be seen &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'&gt;here&lt;/scene&gt;. The axial coordination position is initially occupied by a water molecule. Upon binding of CTAD, this water molecule is released, opening a coordination site for oxygen to bind.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.<br /> <br /> ===3D structures of HIF===<br /> <br /> [[Hypoxia-inducible factor]]<br /> <br /> ==Additional Resources==<br /> For additional information, see: [[Cancer]]<br /> &lt;br /&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1329716 2011-12-07T18:47:02Z

<p>John Hangasky: /* Active Site */</p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/6'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'&gt;active site ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1329715 2011-12-07T18:44:33Z

<p>John Hangasky: /* Active Site */</p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/5'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'&gt;active site ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1329714 2011-12-07T18:42:09Z

<p>John Hangasky: /* Active Site */</p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/6'&gt;active site ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.</div>

John Hangasky https://proteopedia.org/index.php?title=Molecular_Playground/FIH&diff=1329707 2011-12-07T18:17:27Z

<p>John Hangasky: </p> <hr /> <div>{{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]] }}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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 (&lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;) 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.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; Histidines are colored blue, Aspartate is colored red, Iron is the white sphere, and α-KG is colored yellow. The sixth coordination site is initially occupied by a water molecule. Upon binding of CTAD, this water molecule is released, opening a coordination site for oxygen to bind.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.<br /> <br /> ===3D structures of HIF===<br /> <br /> [[Hypoxia-inducible factor]]<br /> <br /> ==Additional Resources==<br /> For additional information, see: [[Cancer]]<br /> &lt;br /&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=Molecular_Playground/FIH&diff=1329693 2011-12-07T18:09:43Z

<p>John Hangasky: /* Active Site */</p> <hr /> <div>{{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]] }}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; Histidines are colored blue, Aspartate is colored red, Iron is the white sphere, and α-KG is colored yellow. The sixth coordination site is initially occupied by a water molecule. Upon binding of CTAD, this water molecule is released, opening a coordination site for oxygen to bind.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.<br /> <br /> ===3D structures of HIF===<br /> <br /> [[Hypoxia-inducible factor]]<br /> <br /> ==Additional Resources==<br /> For additional information, see: [[Cancer]]<br /> &lt;br /&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=Molecular_Playground/FIH&diff=1329592 2011-12-07T17:42:09Z

<p>John Hangasky: </p> <hr /> <div> {{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]] }}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.<br /> <br /> ===3D structures of HIF===<br /> <br /> [[Hypoxia-inducible factor]]<br /> <br /> ==Additional Resources==<br /> For additional information, see: [[Cancer]]<br /> &lt;br /&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=Molecular_Playground/FIH&diff=1329582 2011-12-07T17:39:48Z

<p>John Hangasky: </p> <hr /> <div> {{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]] }}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; (JH) of FIH is shown.<br /> <br /> ===3D structures of HIF===<br /> <br /> [[Hypoxia-inducible factor]]<br /> <br /> ==Additional Resources==<br /> For additional information, see: [[Cancer]]<br /> &lt;br /&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1329550 2011-12-07T17:29:35Z

<p>John Hangasky: /* Active Site */</p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_2&diff=1108362 2010-07-30T18:37:16Z

<p>John Hangasky: New page: &lt;applet load=&#039;2FCT&#039; size=&#039;300&#039; frame=&#039;true&#039; align=&#039;right&#039; caption=&#039;Insert caption here&#039; /&gt;</p> <hr /> <div>&lt;applet load='2FCT' size='300' frame='true' align='right' caption='Insert caption here' /&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky&diff=1108361 2010-07-30T18:36:45Z

<p>John Hangasky: </p> <hr /> <div>*[[User:John Hangasky/Sandbox 1]]<br /> <br /> *[[User:John Hangasky/Sandbox 2]]<br /> <br /> Chemistry Graduate Student at UMass-Amherst and a member of the CBI program.</div>

John Hangasky https://proteopedia.org/index.php?title=CBI_Molecules&diff=1082148 2010-04-30T19:02:44Z

<p>John Hangasky: </p> <hr /> <div>These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].<br /> Many of the molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground]. Follow the links below to read nontechnical descriptions in Proteopedia.<br /> <br /> UMass CBI Members, add your molecules to the list; follow the instructions below the list.<br /> <br /> <br /> '''[[Molecular Playground/Bacterial Chemotaxis Receptors]]''', Thompson &amp; Weis laboratories<br /> <br /> '''[[6-deoxyerythronolide B synthase (DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]''', Schnarr lab (Tsung-Yi Lin)<br /> <br /> '''[[Molecular Playground/Lysozime ]]''', Daniella Gonzalez<br /> <br /> '''[[Molecular Playground/Beta-galactosidase]]''', Judy Ventura<br /> <br /> '''[[Molecular Playground/TRAIL]]''', Charley Swofford<br /> <br /> '''[[Molecular Playground/Taxol]]''', Rohan Patil<br /> <br /> '''[[Molecular Playground/Human Protective Protein Cathepsin A]]''', Yadilette Rivera-Colon<br /> <br /> '''[[Molecular Playground/YKL-40]]''', Ralph A. Francescone III<br /> <br /> '''[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]''', Rotello lab (Daniel Moyano-Marino)<br /> <br /> '''[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]''', Krishna Reddy Raghupathi<br /> <br /> '''[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]''', Rami Rajasekar Reddy<br /> <br /> '''[[Molecular_Playground/ERMan1]]''', Johan Sunryd<br /> <br /> '''[[Molecular Playground/Insulin]]''', Whitney Stoppel<br /> <br /> '''[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]''', Ankit Vahia<br /> <br /> '''[[Human PPCA|Molecular Playground/Human PPCA]]''', Nilima Kolli<br /> <br /> '''[[Molecular Playground/Alginate]]''', David Griffin<br /> <br /> '''[[Molecular Playground/Glutamate Receptor]]''', Chambers Lab (Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano)<br /> <br /> '''[[Molecular Playground/Biotin binding avidin]]''', Diego Amado<br /> <br /> <br /> '''[[Molecular Playground/FIH]]''', Knapp Lab, (Cornelius Taabazuing, Breanne Holmes, John Hangasky)<br /> <br /> <br /> Instructions:<br /> <br /> '''We plan to award a prize for the best CBI Molecules page and/or scene!'''<br /> <br /> Choose a molecule that is part of your research project.<br /> <br /> 1. If you don't already have one, request a Proteopedia account and log in. If you are new to Proteopedia, click Help in the navigation box on the left to get started.<br /> <br /> 2. Make yourself a sandbox page in which you will develop your CBI Molecule scene and description (Enter &quot;User:your name/sandbox 1&quot; (omit quotes) in the search box, then follow instructions to edit this page. See example [[User:Lynmarie K Thompson/Sandbox 1]]). <br /> <br /> 3. Follow the format of the sample CBI molecule page [[Molecular Playground/Bacterial Chemotaxis Receptors]]. Easiest way to do this is to copy this page (in editing mode), paste it into your sandbox page, keep the first paragraph about CBI molecules, and then edit to describe and display your molecule. Your goal is to make this an interesting, nontechnical description of the molecule. If multiple people in one group work on the same molecule, you can each make different scenes for the same CBI molecule and each describe them on the same proteopedia page. Talk with each other about your plans so you are not duplicating efforts.<br /> <br /> 4. Create an attractive scene for your molecule: use the scene authoring tools in the edit mode to create the view you like, then copy the wiki text into your window.<br /> <br /> 5. Follow instructions at [[Molecular Playground/Procedures]] as well. But don't &quot;capture the state script for your scene&quot;; that will be done for you (see #7).<br /> <br /> 6. When you are happy with your sandbox page, make yourself a permanent Proteopedia page, which will be editable by others. Enter &quot;Molecular Playground/your molecule&quot; (omit quotes) in the search box, then follow the instructions to create a new page with this title. Copy the content of your sandbox to this new page.<br /> <br /> 7. When you have finished the final version of your page and scene, edit this CBI Molecules page to add a listing and link for your molecule, following the &quot;Bacterial chemotaxis receptors&quot; example above. Once this link is there, your scene is considered done, and someone will capture the state script for display on the Molecular Playground.<br /> [[Link title]]</div>

John Hangasky https://proteopedia.org/index.php?title=Molecular_Playground/FIH&diff=1082147 2010-04-30T18:58:54Z

<p>John Hangasky: New page: {{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}} === Factor Inhibiting HIF === &#039;&#039;&#039;H&#039;&#039;&#039;ypoxia &#039;&#039;&#039;I&#039;&#039;&#039;nducible &#039;&#039;&#039;F&#039;&#039;&#039;actor (HIF)is a transcription activator that re...</p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082145 2010-04-30T18:55:51Z

<p>John Hangasky: /* Enzyme Surface */</p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is shown.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082144 2010-04-30T18:55:30Z

<p>John Hangasky: /* Active Site */</p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is seen.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082142 2010-04-30T18:51:10Z

<p>John Hangasky: /* Factor Inhibiting HIF */</p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, is colored teal in this depiction.<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is seen.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082129 2010-04-30T18:26:18Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal activation domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, colored teal. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is seen.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082128 2010-04-30T18:24:33Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal activation domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, colored teal. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Enzyme Surface ===<br /> <br /> In this depiction, the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/4'&gt;solvent accessible surface&lt;/scene&gt; of FIH is seen.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082121 2010-04-30T18:14:20Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal activation domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, colored teal. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Enzyme Surface ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082116 2010-04-30T18:09:56Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal activation domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/5'&gt;CTAD&lt;/scene&gt;, colored teal. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082111 2010-04-30T18:07:32Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal activation domain (CTAD) of HIF. This binding domain, &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/2'&gt;CTAD&lt;/scene&gt;, colored teal. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082109 2010-04-30T18:05:38Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/4}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal activation domain (CTAD) of HIF. &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/2'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. In the depiction of the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082107 2010-04-30T18:03:25Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/3}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> FIH binds to the C-terminal activation domain (CTAD) of HIF. &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/2'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. In the depiction of the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082100 2010-04-30T17:55:25Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. In the depiction of the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082097 2010-04-30T17:52:35Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. In the depiction of the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands,/5'&gt;FIH Active Site Ligands&lt;/scene&gt; 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.<br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082096 2010-04-30T17:48:09Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082092 2010-04-30T17:45:48Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/5'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082089 2010-04-30T17:41:14Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/4'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082085 2010-04-30T17:34:10Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site_ligands/3'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082083 2010-04-30T17:30:20Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082082 2010-04-30T17:28:39Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site&lt;/scene&gt; contains an 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. <br /> <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082081 2010-04-30T17:26:15Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site Ligands&lt;/scene&gt; contains an 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. <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082080 2010-04-30T17:23:50Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site Ligands&lt;/scene&gt; contains an 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. <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1082079 2010-04-30T17:16:41Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; contains an 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. <br /> <br /> &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/4'&gt;FIH Active Site Ligands&lt;/scene&gt;<br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081914 2010-04-30T00:32:09Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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. <br /> <br /> === Active Site===<br /> <br /> The &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; contains an 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. <br /> <br /> === Oxygen Channel ===<br /> <br /> 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081911 2010-04-30T00:25:43Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> '''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.<br /> <br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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. <br /> An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081910 2010-04-30T00:25:11Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> '''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.<br /> <br /> === Factor Inhibiting HIF ===<br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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. <br /> An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081905 2010-04-30T00:21:44Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=User:John_Hangasky/Sandbox_1/Fih/2}}<br /> <br /> '''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.<br /> <br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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. <br /> An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081901 2010-04-30T00:18:54Z

<p>John Hangasky: </p> <hr /> <div>{{STRUCTURE_1h2l| PDB=1h2l | SCENE=Fih/1 }}<br /> <br /> '''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.<br /> <br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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. <br /> An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081695 2010-04-28T21:38:03Z

<p>John Hangasky: </p> <hr /> <div>&lt;applet load='FIH_activesite' size='300' frame='true' align='right' caption='Insert caption here' /&gt;<br /> <br /> '''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.<br /> <br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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. <br /> An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081694 2010-04-28T21:37:33Z

<p>John Hangasky: </p> <hr /> <div>&lt;applet load='FIH_activesite.PDB' size='300' frame='true' align='right' caption='Insert caption here' /&gt;<br /> <br /> '''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.<br /> <br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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. <br /> An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081692 2010-04-28T21:36:11Z

<p>John Hangasky: </p> <hr /> <div>&lt;applet load='1h2l' size='300' frame='true' align='right' caption='Insert caption here' /&gt;<br /> <br /> '''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.<br /> <br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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. <br /> An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081690 2010-04-28T21:35:27Z

<p>John Hangasky: </p> <hr /> <div>&lt;applet load='1h2l' size='300' frame='true' align='right' caption='Insert caption here' /&gt;<br /> <br /> '''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.<br /> <br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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. <br /> An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, leading to this active site. <br /> <br /> <br /> <br /> Factor inhibiting HIF &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/2'&gt;(FIH)&lt;/scene&gt; is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081686 2010-04-28T21:29:48Z

<p>John Hangasky: </p> <hr /> <div>&lt;applet load='1h2l' size='300' frame='true' align='right' caption='Insert caption here' /&gt;<br /> <br /> '''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.<br /> <br /> <br /> 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. <br /> For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; 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 &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, and studies are under way, testing this proposed channel.<br /> &lt;nowiki&gt;Insert non-formatted text here&lt;/nowiki&gt;<br /> <br /> <br /> Factor inhibiting HIF &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/2'&gt;(FIH)&lt;/scene&gt; is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body.</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081666 2010-04-28T20:45:42Z

<p>John Hangasky: </p> <hr /> <div>&lt;applet load='1h2l' size='300' frame='true' align='right' caption='Insert caption here' /&gt;<br /> <br /> '''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 2-oxygluatarate dependent aspariginyl hydroxylase that regulates HIF.<br /> <br /> Factor inhibiting HIF &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/2'&gt;(FIH)&lt;/scene&gt; is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body. <br /> <br /> <br /> In normoxic conditions, molecular oxygen is used to hydroxylate HIF, preventing HIF to bind to p300 transcription coactivator. However, in hypoxic environments, this hydroxylation does not occur. For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; at the iron core. An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, and studies are under way, testing this proposed channel.<br /> &lt;nowiki&gt;Insert non-formatted text here&lt;/nowiki&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081651 2010-04-28T20:14:26Z

<p>John Hangasky: </p> <hr /> <div>&lt;applet load='1h2l' size='300' frame='true' align='right' caption='Insert caption here' /&gt;<br /> <br /> Factor inhibiting HIF &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/2'&gt;(FIH)&lt;/scene&gt; is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body. In normoxic conditions, molecular oxygen is used to hydroxylate HIF, preventing HIF to bind to p300. However, in hypoxic environments, this hydroxylation does not occur. For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; at the iron core. An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, and studies are under way, testing this proposed channel.<br /> &lt;nowiki&gt;Insert non-formatted text here&lt;/nowiki&gt;</div>

John Hangasky https://proteopedia.org/index.php?title=User:John_Hangasky/Sandbox_1&diff=1081648 2010-04-28T20:12:22Z

<p>John Hangasky: </p> <hr /> <div><br /> <br /> <br /> Factor inhibiting HIF &lt;scene name='User:John_Hangasky/Sandbox_1/Fih/2'&gt;(FIH)&lt;/scene&gt; is a non-heme iron 2-oxygluatarate dependent dioxygenase, that is responsible for oxygen sensing in the body. In normoxic conditions, molecular oxygen is used to hydroxylate HIF, preventing HIF to bind to p300. However, in hypoxic environments, this hydroxylation does not occur. For this sensing to occur, molecular oxygen must reach the &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_active_site/3'&gt;FIH active site&lt;/scene&gt; at the iron core. An &lt;scene name='User:John_Hangasky/Sandbox_1/Fih_surface/3'&gt;Oxygen Channel&lt;/scene&gt; has been proposed, and studies are under way, testing this proposed channel.</div>

John Hangasky