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Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex
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Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex
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Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex
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Journal Article
Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex
2012
Overview
The circadian clock in mammals is driven by an autoregulatory transcriptional feedback mechanism that takes approximately 24 hours to complete. A key component of this mechanism is a heterodimeric transcriptional activator consisting of two basic helix-loop-helix PER-ARNT-SIM (bHLH-PAS) domain protein subunits, CLOCK and BMAL1. Here, we report the crystal structure of a complex containing the mouse CLOCK:BMAL1 bHLH-PAS domains at 2.3 Å resolution. The structure reveals an unusual asymmetric heterodimer with the three domains in each of the two subunits—bHLH, PAS-A, and PAS-B—tightly intertwined and involved in dimerization interactions, resulting in three distinct protein interfaces. Mutations that perturb the observed heterodimer interfaces affect the stability and activity of the CLOCK:BMAL1 complex as well as the periodicity of the circadian oscillator. The structure of the CLOCK:BMAL1 complex is a starting point for understanding at an atomic level the mechanism driving the mammalian circadian clock.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Animals
/ ARNTL Transcription Factors - chemistry
/ ARNTL Transcription Factors - genetics
/ ARNTL Transcription Factors - metabolism
/ Binding
/ Biological and medical sciences
/ Clocks
/ Cranes
/ DNA
/ Fundamental and applied biological sciences. Psychology
/ Humans
/ Mammals
/ Mice
/ Mutant Proteins - metabolism
/ Mutation
/ Protein Interaction Domains and Motifs
/ Protein Structure, Quaternary
/ Protein Structure, Secondary
/ Protein Subunits - chemistry
/ Protein Subunits - metabolism
/ protein-protein interactions
/ Proteins
