Asymmetric Mode of Ca2+-S100A4 Interaction with Nonmuscle Myosin IIA Generates Nanomolar Affinity Required for Filament Remodeling

@inproceedings{Elliott2012AsymmetricMO,
  title={Asymmetric Mode of Ca2+-S100A4 Interaction with Nonmuscle Myosin IIA Generates Nanomolar Affinity Required for Filament Remodeling},
  author={Paul Ronald Elliott and Andrew F. Irvine and Hyun Suk Jung and Kaeko Tozawa and Martyna W. Pastok and Remigio Picone and Sandip K. Badyal and Jaswir Basran and Philip S. Rudland and Roger Barraclough and Lu-Yun Lian and Clive R. Bagshaw and Marina Kriajevska and Igor L. Barsukov},
  booktitle={Structure},
  year={2012}
}
Filament assembly of nonmuscle myosin IIA (NMIIA) is selectively regulated by the small Ca²⁺-binding protein, S100A4, which causes enhanced cell migration and metastasis in certain cancers. Our NMR structure shows that an S100A4 dimer binds to a single myosin heavy chain in an asymmetrical configuration. NMIIA in the complex forms a continuous helix that stretches across the surface of S100A4 and engages the Ca²⁺-dependent binding sites of each subunit in the dimer. Synergy between these sites… CONTINUE READING

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