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Commentary

Assembly and function of bHLH–PAS complexes

Jennifer L. Fribourgh and Carrie L. Partch
  1. aDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, CA 96054;
  2. bCenter for Circadian Biology, University of California, San Diego, CA 92161

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PNAS May 23, 2017 114 (21) 5330-5332; first published May 15, 2017; https://doi.org/10.1073/pnas.1705408114
Jennifer L. Fribourgh
aDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, CA 96054;
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Carrie L. Partch
aDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, CA 96054;
bCenter for Circadian Biology, University of California, San Diego, CA 92161
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  • For correspondence: cpartch@ucsc.edu
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    Fig. 1.

    The global architecture of bHLH–PAS heterodimers. From Left to Right, the structure of ARNT-containing complexes: AHR–ARNT bound to DNA encoding the DRE (PDB ID code 5V0L), NPAS3–ARNT bound to DNA encoding the HRE (PDB ID code 5SY7), and HIF1-α–ARNT bound to the HRE (PDB ID code HZPR). On the far right, the CLOCK–BMAL1 bHLH–PAS structure (PDB ID code 4F3L) is aligned to the bHLH domain of the CLOCK–BMAL1 bHLH–E-box DNA structure (PDB ID code 4H10).

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Assembly and function of bHLH–PAS complexes
Jennifer L. Fribourgh, Carrie L. Partch
Proceedings of the National Academy of Sciences May 2017, 114 (21) 5330-5332; DOI: 10.1073/pnas.1705408114

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Assembly and function of bHLH–PAS complexes
Jennifer L. Fribourgh, Carrie L. Partch
Proceedings of the National Academy of Sciences May 2017, 114 (21) 5330-5332; DOI: 10.1073/pnas.1705408114
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  • Structural study of AHR/ARNT/DRE complex
    - Apr 10, 2017
Proceedings of the National Academy of Sciences: 114 (21)
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