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Biophys J. 2016 Jun 7;110(11):2517-2527. doi: 10.1016/j.bpj.2016.04.048.

Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection.

Author information

1
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
2
Minnesota NMR Center, University of Minnesota, Minneapolis, Minnesota.
3
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois. Electronic address: rrock@uchicago.edu.

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.

PMID:
27276269
PMCID:
PMC4906270
DOI:
10.1016/j.bpj.2016.04.048
[Indexed for MEDLINE]
Free PMC Article

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