Divalent cations induce a compaction of intrinsically disordered myelin basic protein

作者：Baran Christian; Smith Graham S T; Bamm Vladimir V; Harauz George; Lee Jeremy S^*

来源：Biochemical and Biophysical Research Communications, 2010, 391(1): 224-229.

DOI：10.1016/j.bbrc.2009.11.036

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

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.

• 出版日期2010-1-1