title: Divalent cations induce a compaction of intrinsically disordered myelin basic protein.
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 18.5kDa. 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.
authors.affiliation: Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask, Canada.
authors.forename: Christian
authors.initials: C
authors.lastname: Baran
authors.forename: Graham S T
authors.initials: GS
authors.lastname: Smith
authors.forename: Vladimir V
authors.initials: VV
authors.lastname: Bamm
authors.forename: George
authors.initials: G
authors.lastname: Harauz
authors.forename: Jeremy S
authors.initials: JS
authors.lastname: Lee
mesh_terms: D000818:Animals; D002413:Cations, Divalent / Q000737:chemistry; D003300:Copper / Q000737:chemistry*; D051379:Mice; D004676:Myelin Basic Protein; D049329:Nanostructures; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics; D016062:Porosity; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics; D015032:Zinc / Q000737:chemistry*
chemical_list: D002413:Cations, Divalent; C499047:Mbp protein, mouse; D004676:Myelin Basic Protein; D009419:Nerve Tissue Proteins; D011994:Recombinant Proteins; D014157:Transcription Factors; D003300:Copper; D015032:Zinc