Myelin basic protein has multiple calmodulin-binding sites

David S. Libich, Christopher M.D. Hill, Jeffery D. Haines, George Harauz

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

Myelin basic protein (MBP) has been shown to bind calmodulin (CaM) in a specific Ca2+-dependent manner via a primary target sequence at its C-terminus [Protein Sci. 12 (2003) 1507]. Upon deimination of MBP, the nature of the interaction changed significantly, suggesting either a new binding site or different conformers with different affinities for CaM. In order to resolve this issue, we investigated here the CaM-binding properties of N- and C-terminal deletion mutants of MBP using Trp fluorescence spectroscopy and mass spectrometry. We conclude that there is an additional CaM-binding site on MBP in a central segment (we posit murine residues 82-93) that forms an amphipathic α-helix.

Original languageEnglish (US)
Pages (from-to)313-319
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume308
Issue number2
DOIs
StatePublished - Aug 22 2003
Externally publishedYes

Keywords

  • Acrylamide quenching
  • Calmodulin
  • Fluorescence spectroscopy
  • Mass spectroscopy
  • Myelin basic protein

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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