A structural view of plant CRY2 photoactivation and inactivation

Cryptochrome (CRY) photoreceptors undergo photoresponsive homo-oligomerization to become physiologically active, and BICs (blue-light inhibitors of CRYs) suppress homo-oligomerization. Structural elucidation of CRY–CRY homo-oligomers and a CRY–BIC heterodimer reveals how the activity of plant CRYs is regulated by alternative protein–protein interactions.

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Fig. 1: Photoactivation and inactivation of plant cryptochromes.
Fig. 2: Structural insights into CRY2 inactivation.


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Work in the authors’ laboratories is supported in part by the National Natural Science Foundation of China (31970265 to Q.W.), the Natural Science Foundation of Fujian Province (2019J06014 to Q.W.) and the National Institutes of Health (GM56265 to C.L.).

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Correspondence to Chentao Lin.

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Wang, Q., Lin, C. A structural view of plant CRY2 photoactivation and inactivation. Nat Struct Mol Biol 27, 401–403 (2020).

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