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Model for the regulation of mCRY1 binding by Lys-537BMAL1 acetylation. Top, in its non-acetylated state, Lys-537 masks negative charges in mBMAL1 through intramolecular interactions and thereby interferes with mCRY1 binding. Bottom, Lys-537 acetylation unmasks negative mBMAL1 charges and allows for electrostatic interactions with positively charged mCRY1 residues predominantly in its tail region.
