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Interaction of Circadian Clock Proteins CRY1 and PER2 Is Modulated by Zinc Binding and Disulfide Bond Formation
Zinc binding and disulfide bonds influence how key body clock proteins CRY1 and PER2 interact
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Abstract
The crystal structure of a complex between mouse CRY1 and mouse PER2 reveals an unexpected zinc ion stabilizing their interactions.
- Mammalian CRY/PER complexes play a key role in regulating the circadian clock.
- The crystal structure shows mPER2 wrapping around mCRY1, affecting binding sites for regulatory proteins.
- Zinc binding is essential for stabilizing the mCRY1-mPER2 interaction in living cells.
- The formation of the mCRY1/mPER2 complex may be influenced by the cell's redox state.
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