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...

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Main Authors: Wu, D, Rastinejad, F
Format: Journal article
Language:English
Published: 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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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