植物 CRY2 光激活和失活的结构观点。
A structural view of plant CRY2 photoactivation and inactivation.
机构信息
Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University, Fuzhou, China.
Department of Molecular, Cell and Developmental Biology, University of California, Los Angeles, CA, USA.
出版信息
Nat Struct Mol Biol. 2020 May;27(5):401-403. doi: 10.1038/s41594-020-0432-6.
Abstract
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.
摘要
隐花色素（CRY）光受体发生光响应同源寡聚化，从而具有生理活性，而 BICs（CRY 的蓝光抑制剂）则抑制同源寡聚化。CRY–CRY 同源寡聚体和 CRY–BIC 异源二聚体的结构阐明揭示了植物 CRYs 的活性如何通过替代的蛋白-蛋白相互作用来调节。
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