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  Interaction of Circadian Clock Proteins CRY1 and PER2 Is Modulated by Zinc Binding and Disulfide Bond Formation

Schmalen, I., Reischl, S., Wallach, T., Klemz, R., Grudziecki, A., Prabu, J. R., et al. (2014). Interaction of Circadian Clock Proteins CRY1 and PER2 Is Modulated by Zinc Binding and Disulfide Bond Formation. CELL, 157(5), 1203-1215. doi:10.1016/j.cell.2014.03.057.

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 Creators:
Schmalen, Ira1, Author              
Reischl, Silke2, Author
Wallach, Thomas2, Author
Klemz, Roman2, Author
Grudziecki, Astrid2, Author
Prabu, J. Rajan1, Author              
Benda, Christian1, Author              
Kramer, Achim2, Author
Wolf, Eva3, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2external, ou_persistent22              
3Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

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Free keywords: CRYPTOCHROME1 TRANSGENIC MICE; CRYSTAL-STRUCTURE; MAMMALIAN CRY1; C-TERMINUS; RHYTHMS; IDENTIFICATION; DEGRADATION; NUCLEUS; CELLS
 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.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: CELL
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 157 (5) Sequence Number: - Start / End Page: 1203 - 1215 Identifier: ISSN: 0092-8674