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- W2416509858 abstract "Coiled-coil fusions are a useful approach to enforce dimerization in protein engineering. However, the final structures of coiled-coil fusion proteins have received relatively little attention. Here, we determine the structural outcome of adjacent parallel and antiparallel coiled coils. The targets are coiled coils that stabilize myosin-10 in single-molecule biophysical studies. We reveal the solution structure of a short, antiparallel, myosin-10 coiled-coil fused to the parallel GCN4-p1 coiled coil. Surprisingly, this structure is a continuous, antiparallel coiled coil where GCN4-p1 pairs with myosin-10 rather than itself. We also show that longer myosin-10 segments in these parallel/antiparallel fusions are dynamic and do not fold cooperatively. Our data resolve conflicting results on myosin-10 selection of actin filament bundles, demonstrating the importance of understanding coiled-coil orientation and stability." @default.
- W2416509858 created "2016-06-24" @default.
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- W2416509858 creator A5044788584 @default.
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- W2416509858 date "2016-06-01" @default.
- W2416509858 modified "2023-09-26" @default.
- W2416509858 title "Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection" @default.
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- W2416509858 doi "https://doi.org/10.1016/j.bpj.2016.04.048" @default.
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