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Structure of the S100A4/myosin-IIA complex.

Udupi A Ramagopal1, Natalya G Dulyaninova, Kristen M Varney

  • 1Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. anne.bresnick@einstein.yu.edu.

BMC Structural Biology
|November 21, 2013
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The S100A4 protein binds to myosin-IIA, causing it to disassemble. Structural studies reveal how S100A4 interacts with myosin-IIA, suggesting that coiled-coil instability aids this process.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • S100A4, a calcium-binding protein, regulates cell motility by affecting cellular protrusions.
  • S100A4 is known to bind and disassemble myosin-IIA filaments, but the mechanism remains unclear.

Purpose of the Study:

  • To elucidate the structural mechanism of S100A4 binding to myosin-IIA.
  • To understand how S100A4 mediates myosin-IIA depolymerization.

Main Methods:

  • X-ray crystallography of the S100A4/myosin-IIA peptide complex.
  • Nuclear Magnetic Resonance (NMR) spectroscopy with spin-labeled peptides.
  • Biophysical studies of complex formation with dimeric myosin-IIA.

Main Results:

  • Determined the crystal structure revealing an asymmetric binding mode of the myosin-IIA peptide to the S100A4 dimer.
  • NMR confirmed the asymmetric binding and orientation.
  • S100A4 binding dissociates myosin-IIA dimers into a complex with a single myosin-IIA chain.
  • Myosin-IIA coiled-coil instability facilitates S100A4 binding.

Conclusions:

  • The structure reveals atomic details of S100A4 interaction with the myosin-IIA heavy chain.
  • Myosin-IIA residues 1908-1923 form a core binding site for S100A4.
  • Structural fluctuations in the myosin-IIA coiled-coil likely facilitate S100A4 binding to individual myosin-IIA chains.