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  Structures of Drosophila Cryptochrome and Mouse Cryptochrome1 Provide Insight into Circadian Function

Czarna, A., Berndt, A., Singh, H. R., Grudziecki, A., Ladurner, A. G., Timinszky, G., et al. (2013). Structures of Drosophila Cryptochrome and Mouse Cryptochrome1 Provide Insight into Circadian Function. CELL, 153(6), 1394-1405. doi:10.1016/j.cell.2013.05.011.

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 Creators:
Czarna, Anna1, Author              
Berndt, Alex2, Author
Singh, Hari Raj2, Author
Grudziecki, Astrid2, Author
Ladurner, Andreas G.2, Author
Timinszky, Gyula2, Author
Kramer, Achim2, Author
Wolf, Eva2, Author              
Affiliations:
1Holak, Tad / NMR Spectroscopy, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565154              
2external, ou_persistent22              

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Free keywords: LIGHT-DEPENDENT MAGNETOSENSITIVITY; CIRCULAR-DICHROISM SPECTRA; CRYSTAL-STRUCTURE; C-TERMINUS; MAMMALIAN CRY1; 6-4 PHOTOLYASE; FEEDBACK LOOP; CLOCK; PROTEIN; MECHANISM
 Abstract: Drosophila cryptochrome (dCRY) is a FAD-dependent circadian photoreceptor, whereas mammalian cryptochromes (CRY1/2) are integral clock components that repress mCLOCK/mBMAL1-dependent transcription. We report crystal structures of full-length dCRY, a dCRY loop deletion construct, and the photolyase homology region of mouse CRY1 (mCRY1). Our dCRY structures depict Phe534 of the regulatory tail in the same location as the photolesion in DNA-repairing photolyases and reveal that the sulfur loop and tail residue Cys523 plays key roles in the dCRYphotoreaction. OurmCRY1structure visualizes previously characterized mutations, an NLS, and MAPK and AMPK phosphorylation sites. We show that the FAD and antenna chromophore-binding regions, a predicted coiled-coil helix, the C-terminal lid, and charged surfaces are involved in FAD-independent mPER2 and FBXL3 binding and mCLOCK/mBMAL1 transcriptional repression. The structure of a mammalian cryptochrome1 protein may catalyze the development of CRY chemical probes and the design of therapeutic metabolic modulators.

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Language(s): eng - English
 Dates: 2013
 Publication Status: Published in print
 Pages: 12
 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: 153 (6) Sequence Number: - Start / End Page: 1394 - 1405 Identifier: ISSN: 0092-8674