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dCRY mediates light synchronization of the fly circadian master clock. The C-terminus of dCRY plays an important role in modulating light sensitivity and activity of the protein and it harbours several protein-protein interaction motifs (Linear Motifs: LMs). Co-immunoprecipitation assays and mass spectrometry analysis have revealed that dCRY is bound to NINAC, an element of the fly's visual cascade assembled in a multiprotein signalling complex organized by INAD, a scaffolding protein with 5 structural PDZ domains. Preliminary results demonstrate that dCRY is recognised by the region of INAD which comprises the PDZ2 and PDZ3 domains and includes a predicted Calmodulin-binding motif. Aim of this research program is the NMR characterization of the interaction between dCRY and INAD. To this purpose, we will use NMR chemical shift mapping and 15N relaxation measurements to study the interaction of the aforementioned INAD fragment with suitable LM-containing peptides derived from dCRY.
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