Hypoxia-Inducible Factors
From Proteopedia
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| - | '''Hypoxia-inducible factors''' (HIFs) are transcription factors responsible for the induction of genes involved in the adaptation to decreases in oxygen availability, known as [https://en.wikipedia.org/wiki/Hypoxia_(medical) hypoxia]. | ||
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<Structure load='6E3U' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='6E3U' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
| + | '''Hypoxia-inducible factors''' ('''HIFs''') are transcription factors responsible for the induction of genes involved in the adaptation to decreases in oxygen availability, known as [https://en.wikipedia.org/wiki/Hypoxia_(medical) hypoxia]. | ||
==Structure== | ==Structure== | ||
| + | HIFs are heterodimeric complexes that form part of the basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) family of proteins. All subunits are similar in structure and can contain the following domains from the N-terminus to the C-terminus: | ||
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| + | * '''bHLH''': important for heterodimer formation and DNA binding to Hypoxia Response Elements (HRE) | ||
| + | * '''PAS''': helps with heterodimerization | ||
| + | * Oxygen-dependent degradation domain ('''ODDD'''): mediates oxygen-regulated stability. It contains two Proline (P) residues susceptible of hydroxylation and one Lysine (L) that can be acetylated | ||
| + | * N-terminal and C-terminal transactivating domains ('''N-TAD''' and '''C-TAD'''): bind different coactivators to promote gene expression | ||
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| + | HIF complexes are made of a constitutively expressed subunit HIF-β and an oxygen-regulated subunit, which can be HIF-1α or its paralogs HIF-2α and HIF-3α. the stability and activity of the α subunit is regulated by post-translational modifications such as hydroxilation, ubiquitination, acetylation and phosphorylation. HIF-1β is also known as the aryl hydrocarbon nuclear translocator (ARNT). | ||
==Your Heading Here (maybe something like 'Structure')== | ==Your Heading Here (maybe something like 'Structure')== | ||
| - | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
This is a default text for your page '''Gonzalo Garcia-Martin/Sandbox1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Gonzalo Garcia-Martin/Sandbox1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
Revision as of 12:50, 13 November 2020
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Hypoxia-inducible factors (HIFs) are transcription factors responsible for the induction of genes involved in the adaptation to decreases in oxygen availability, known as hypoxia.
Contents |
Structure
HIFs are heterodimeric complexes that form part of the basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) family of proteins. All subunits are similar in structure and can contain the following domains from the N-terminus to the C-terminus:
- bHLH: important for heterodimer formation and DNA binding to Hypoxia Response Elements (HRE)
- PAS: helps with heterodimerization
- Oxygen-dependent degradation domain (ODDD): mediates oxygen-regulated stability. It contains two Proline (P) residues susceptible of hydroxylation and one Lysine (L) that can be acetylated
- N-terminal and C-terminal transactivating domains (N-TAD and C-TAD): bind different coactivators to promote gene expression
HIF complexes are made of a constitutively expressed subunit HIF-β and an oxygen-regulated subunit, which can be HIF-1α or its paralogs HIF-2α and HIF-3α. the stability and activity of the α subunit is regulated by post-translational modifications such as hydroxilation, ubiquitination, acetylation and phosphorylation. HIF-1β is also known as the aryl hydrocarbon nuclear translocator (ARNT).
Your Heading Here (maybe something like 'Structure')
This is a default text for your page Gonzalo Garcia-Martin/Sandbox1. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
Proteopedia Page Contributors and Editors (what is this?)
Gonzalo Garcia-Martin, Michal Harel, Carmen Paredes Yubero, Rocío Moreno
