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Divalent cations induce a compaction of intrinsically disordered myelin basic protein

Christian Baran1, Graham S T Smith, Vladimir V Bamm

  • 1Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask, Canada.

Biochemical and Biophysical Research Communications
|November 12, 2009
PubMed

Insights

Copper and zinc ions compact the myelin basic protein (MBP), an intrinsically disordered protein. This finding suggests a potential tertiary structure relevant to MBP

Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Central nervous system (CNS) myelin is a crucial insulating layer formed by oligodendrocytes, enabling rapid nerve impulse transmission.
  • Myelin basic protein (MBP) is a major component of CNS myelin, predominantly existing as the 18.5kDa splice isoform in mature myelin.
  • In solution, MBP is an intrinsically disordered protein with a flexible structure, facilitating various molecular interactions.

Purpose of the Study:

  • To investigate the structural changes of myelin basic protein (MBP) in the presence of divalent cations.
  • To explore the potential tertiary conformation of MBP induced by metal ions, possibly reflecting its in-myelin arrangement.

Main Methods:

  • Utilizing nanopore analysis to study protein structure.
  • In vitro experiments to observe MBP behavior under specific ionic conditions.

Main Results:

  • Divalent cations, specifically copper (Cu2+) and zinc (Zn2+), were observed to induce compaction of the extended MBP structure in vitro.
  • The observed compaction suggests the formation of a more ordered tertiary conformation.

Conclusions:

  • Divalent cations like copper and zinc can significantly alter the conformation of myelin basic protein.
  • These structural changes may provide insights into the arrangement and function of MBP within the complex myelin sheath.

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