4CT0

Crystal Structure of Mouse Cryptochrome1 in Complex with Period2

4CT0 の概要

• エントリーDOI: 10.2210/pdb4ct0/pdb
• 分子名称: CRYPTOCHROME-1, PERIOD CIRCADIAN PROTEIN HOMOLOG 2, ZINC ION, ... (6 entities in total)
• 機能のキーワード: circadian clock protein, cryptochrome-period complex, cryptochrome interactions, zinc interface, disulfide bond, redox regulation
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE); 詳細
• 細胞内の位置: Cytoplasm: P97784; Nucleus: O54943
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75197.45

構造登録者

Schmalen, I.,Rajan Prabu, J.,Benda, C.,Wolf, E. (登録日: 2014-03-11, 公開日: 2014-06-04, 最終更新日: 2023-12-20)

主引用文献

Schmalen, I.,Reischl, S.,Wallach, T.,Klemz, R.,Grudziecki, A.,Prabu, J.R.,Benda, C.,Kramer, A.,Wolf, E.
Interaction of Circadian Clock Proteins Cry1 and Per2 is Modulated by Zinc Binding and Disulfide Bond Formation.
Cell(Cambridge,Mass.), 157:1203-, 2014

PubMed Abstract: Period (PER) proteins are essential components of the mammalian circadian clock. They form complexes with cryptochromes (CRY), which negatively regulate CLOCK/BMAL1-dependent transactivation of clock and clock-controlled genes. To define the roles of mammalian CRY/PER complexes in the circadian clock, we have determined the crystal structure of a complex comprising the photolyase homology region of mouse CRY1 (mCRY1) and a C-terminal mouse PER2 (mPER2) fragment. mPER2 winds around the helical mCRY1 domain covering the binding sites of FBXL3 and CLOCK/BMAL1, but not the FAD binding pocket. Our structure revealed an unexpected zinc ion in one interface, which stabilizes mCRY1-mPER2 interactions in vivo. We provide evidence that mCRY1/mPER2 complex formation is modulated by an interplay of zinc binding and mCRY1 disulfide bond formation, which may be influenced by the redox state of the cell. Our studies may allow for the development of circadian and metabolic modulators.

PubMed: 24855952
DOI: 10.1016/J.CELL.2014.03.057

実験手法

X-RAY DIFFRACTION (2.45 Å)