Structural characterization of mammalian bHLH-PAS transcription factors
The mammalian basic helix-loop-helix-PER-ARNT-SIM (bHLH–PAS) transcription factors share common architectural features that include a bHLH DNA-binding domain and tandemly positioned PAS domains. The sixteen members of this family include the hypoxia-inducible factors (HIF-1α and HIF-2α), ARNT (also...
Main Authors: | , |
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Format: | Journal article |
Language: | English |
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Elsevier
2016
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author | Wu, D Rastinejad, F |
author_facet | Wu, D Rastinejad, F |
author_sort | Wu, D |
collection | OXFORD |
description | The mammalian basic helix-loop-helix-PER-ARNT-SIM (bHLH–PAS) transcription factors share common architectural features that include a bHLH DNA-binding domain and tandemly positioned PAS domains. The sixteen members of this family include the hypoxia-inducible factors (HIF-1α and HIF-2α), ARNT (also known as HIF-1β), CLOCK and BMAL1. Most bHLH-PAS proteins have been genetically linked to variety of diseases in humans, including cancers, metabolic syndromes and psychiatric conditions. To function as transcription factors, the bHLH-PAS proteins must form heterodimeric complexes. Recent crystallographic studies of HIF-α-ARNT and CLOCK-BMAL1 complexes have unveiled the organization of their multi-domain bHLH-PAS-A-PAS-B segments, revealing how these architectures can give rise to unique patterns of heterodimerization. As our structural understanding becomes better integrated with ligand-discovery and target gene identification, a more comprehensive picture of their architectural and functional properties will emerge.
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first_indexed | 2024-03-07T05:04:42Z |
format | Journal article |
id | oxford-uuid:d981b163-4452-4974-b2fa-96e0b608e475 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T05:04:42Z |
publishDate | 2016 |
publisher | Elsevier |
record_format | dspace |
spelling | oxford-uuid:d981b163-4452-4974-b2fa-96e0b608e4752022-03-27T08:56:28ZStructural characterization of mammalian bHLH-PAS transcription factorsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d981b163-4452-4974-b2fa-96e0b608e475EnglishSymplectic ElementsElsevier2016Wu, DRastinejad, FThe mammalian basic helix-loop-helix-PER-ARNT-SIM (bHLH–PAS) transcription factors share common architectural features that include a bHLH DNA-binding domain and tandemly positioned PAS domains. The sixteen members of this family include the hypoxia-inducible factors (HIF-1α and HIF-2α), ARNT (also known as HIF-1β), CLOCK and BMAL1. Most bHLH-PAS proteins have been genetically linked to variety of diseases in humans, including cancers, metabolic syndromes and psychiatric conditions. To function as transcription factors, the bHLH-PAS proteins must form heterodimeric complexes. Recent crystallographic studies of HIF-α-ARNT and CLOCK-BMAL1 complexes have unveiled the organization of their multi-domain bHLH-PAS-A-PAS-B segments, revealing how these architectures can give rise to unique patterns of heterodimerization. As our structural understanding becomes better integrated with ligand-discovery and target gene identification, a more comprehensive picture of their architectural and functional properties will emerge. |
spellingShingle | Wu, D Rastinejad, F Structural characterization of mammalian bHLH-PAS transcription factors |
title | Structural characterization of mammalian bHLH-PAS transcription factors |
title_full | Structural characterization of mammalian bHLH-PAS transcription factors |
title_fullStr | Structural characterization of mammalian bHLH-PAS transcription factors |
title_full_unstemmed | Structural characterization of mammalian bHLH-PAS transcription factors |
title_short | Structural characterization of mammalian bHLH-PAS transcription factors |
title_sort | structural characterization of mammalian bhlh pas transcription factors |
work_keys_str_mv | AT wud structuralcharacterizationofmammalianbhlhpastranscriptionfactors AT rastinejadf structuralcharacterizationofmammalianbhlhpastranscriptionfactors |