Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex

The crystal structure of the mouse CLOCK:BMAL1 complex was determined at 2.3 Å resolution.

• The CLOCK:BMAL1 complex forms an asymmetric heterodimer with tightly intertwined domains.
• Three distinct protein interfaces are involved in the dimerization of CLOCK and BMAL1.
• Mutations disrupting these interfaces can affect the stability and activity of the complex.
• Altered stability and activity of the CLOCK:BMAL1 complex may influence the circadian oscillator's periodicity.
• The structure provides a foundation for exploring the atomic mechanisms of the mammalian circadian clock.

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