Sandbox Reserved 973: Difference between revisions
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The two peptides involved in the dimere have very similar sequences . In ''mus musculus'' BMAL1 is 387 residues long and CLOCK is 361. | The two peptides involved in the dimere have very similar sequences . In ''mus musculus'' BMAL1 is 387 residues long and CLOCK is 361. | ||
Both of these subunits are basic helix-loop-helix-PAS proteins (bHLH-PAS) which contain the same 3 particular domains: a bHLH domain, a PAS-A domain and a PAS-B domain. They are involved in DNA binding and dimerization abilities. Mutations that affects the heterodimer interfaces can then disturb the activity of the complex and therefore the persistence and periodicity of the circadian cycle. In deed the two subunits are tightly intertwined as each domain of CLOCK interact with the corresponding one of BMAL1. | Both of these subunits are basic helix-loop-helix-PAS proteins (bHLH-PAS) which contain the same 3 particular domains: a bHLH domain, a PAS-A domain and a PAS-B domain. They are involved in DNA binding and dimerization abilities. Mutations that affects the heterodimer interfaces can then disturb the activity of the complex and therefore the persistence and periodicity of the circadian cycle. In deed the two subunits are tightly intertwined as each domain of CLOCK interact with the corresponding one of BMAL1. | ||
Another important feature of this heterodimere is that there is an assymetric distribution of the electrostatic potential. CLOCK tends to have a global negative charge while BMAL1 has a positive one. The fact that the two subunits of the complex expose this charged surface in the 3D structure match with the hypothesis that CLOCK and BMAL1 are not involved in the same interaction with the other regulatory proteins listed before. | |||
