Divalent cations induce a compaction of intrinsically disordered myelin basic protein

  • Baran C
  • Smith G
  • Bamm V
 et al. 
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Abstract

Central nervous system myelin is a dynamic entity arising from membrane processes extended from oligodendrocytes, which form a tightly-wrapped multilamellar structure around neurons. In mature myelin, the predominant splice isoform of classic MBP is 18.5 kDa. In solution, MBP is an extended, intrinsically disordered protein with a large effective protein surface for myriad interactions, and possesses transient and/or induced ordered secondary structure elements for molecular association or recognition. Here, we show by nanopore analysis that the divalent cations copper and zinc induce a compaction of the extended protein in vitro, suggestive of a tertiary conformation that may reflect its arrangement in myelin. © 2009 Elsevier Inc. All rights reserved.

Author-supplied keywords

  • Induced folding
  • Intrinsically disordered protein
  • Multiple sclerosis
  • Myelin basic protein (MBP)
  • Nanopore analysis

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