| Summary: | Proteins containing glutamine repeats (polyQ) are known to be structurally unstable. Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to neurodegenerative disease, a symptom of which are protein aggregates. This has led to extensive research of the structure of polyQ stretches. However, the accumulation of contradictory results suggests that protein context might be of importance. Here we aimed to evaluate the structural context of polyQ regions in proteins by analysing the secondary structure of polyQ proteins and their homologs. The results revealed that the secondary structure in polyQ vicinity is predominantly random coil or helix. Importantly, the regions surrounding the polyQ are often not solved in 3D structures. In the few cases where the point of insertion of the polyQ was mapped to a full protein, we observed that these are always located in the surface of the protein. The findings support the hypothesis that polyQ might serve to extend coiled coils at their C-terminus in highly disordered regions involved in protein-protein interactions.
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