Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex

Author:

Huang Nian1,Chelliah Yogarany23,Shan Yongli2,Taylor Clinton A.14,Yoo Seung-Hee2,Partch Carrie123,Green Carla B.2,Zhang Hong1,Takahashi Joseph S.23

Affiliation:

1. Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

2. Department of Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

3. Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

4. Molecular Biophysics Graduate Program, Division of Basic Science, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Abstract

A Timely Structure The physiology and behavior of most organisms are inextricably aligned with the day/night cycle. In mammals, these daily rhythms are generated by a circadian clock encoded by transcriptional activators and repressors operating in a feedback loop that takes about 24 hours to complete. A key participant in this loop is a heterodimeric transcriptional activator consisting of the CLOCK and BMAL1 proteins. Huang et al. (p. 189 , published online 31 May; see Perspective by Crane ) determined the crystal structure of a complex containing the PAS domains (implicated in protein-protein interactions) and the basic helix-loop-helix domains (implicated in DNA binding) from each protein. CLOCK and BMAL1 were observed to be tightly intertwined in an unusual asymmetric conformation, which may contribute to the stability and activity of the complex.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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