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Biochem Biophys Res Commun. 2014 Aug 8;450(4):1606-11. doi: 10.1016/j.bbrc.2014.07.038. Epub 2014 Jul 12.

Evaluation of the steric impact of flavin adenine dinucleotide in Drosophila melanogaster cryptochrome function.

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  • 1Dept. of Biomedical Sciences, University of Padova, Padova, Italy.
  • 2Dept. of Pharmaceutical and Pharmacological Sciences, University of Padova, Padova, Italy.
  • 3Dept. of Biology, University of Padova, Padova, Italy.
  • 4Dept. of Biomedical Sciences, University of Padova, Padova, Italy. Electronic address:


Photoreceptors are crucial components for circadian rhythm entrainment in animals, plants, fungi and cyanobacteria. Cryptochromes (CRYs) are flavin adenine dinucleotide (FAD) containing photoreceptors, and FAD is responsible for signal transduction, in contrast to photolyases where it promotes DNA-damage repair. In this work, we investigated an alternative role for FAD in CRY. We analyzed the Drosophila melanogaster CRY crystal structure by means of molecular dynamics, elucidating how this large co-factor within the receptor could be crucial for CRY structural stability. The co-factor appears indeed to improve receptor motility, providing steric hindrance. Moreover, multiple sequence alignments revealed that conserved motifs in the C-terminal tail could be necessary for functional stability.


Cryptochrome; Drosophila melanogaster; Flavin adenine dinucleotide; Molecular dynamics; Sequence analysis; Structural bioinformatics

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