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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state

Mumdooh A M Ahmed1, Vladimir V Bamm, Lichi Shi

  • 1Department of Physics, University of Guelph, Guelph, Canada.

Biophysical Journal
|January 13, 2009
PubMed

Insights

Myelin basic protein (MBP) interacts with actin, inducing structural changes in both proteins. This study reveals MBP

Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Myelin basic protein (MBP) is crucial for central nervous system myelin sheath integrity.
  • MBP is an intrinsically disordered protein with multifunctional roles, including structural stabilization and potential signaling.
  • Its interaction with the cytoskeleton is vital for myelin assembly.

Purpose of the Study:

  • To investigate the conformational changes of 18.5 kDa MBP when associated with actin microfilaments.
  • To elucidate the structural basis of MBP's role as a linker and potential signaling hub.

Main Methods:

  • Solid-state NMR (SSNMR) spectroscopy.
  • Fourier transform infrared (FTIR) spectroscopy.
  • Utilized fully (13)C,(15)N-labeled MBP complexed with F-actin.

Main Results:

  • FTIR and SSNMR revealed induced folding in both MBP and actin upon complex formation.
  • MBP exhibited increased alpha-helix and beta-sheet content, while actin showed increased beta-sheet content.
  • MBP in MBP-actin assemblies is structurally heterogeneous, with ordered secondary structures in terminal and central regions.

Conclusions:

  • MBP's conformational polymorphism supports its dual role as a membrane-cytoskeleton linker and a signaling molecule.
  • The induced structural changes highlight the dynamic nature of MBP in cellular interactions.
  • Findings provide insights into the molecular mechanisms underlying myelin structure and function.

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