User:Cornelius Taabazuing/sandbox 1: Difference between revisions

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=== Factor Inhibiting HIF ===

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

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

~~FIH binds to the C-terminal Activation Domain (CTAD) of HIF. This binding domain, <scene name='User:John_Hangasky/Sandbox_1/Fih/5'>CTAD</scene>, (JH)is colored teal in this depiction.~~

=== Active Site===

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