Myelin basic protein has multiple calmodulin-binding sites

Biochem Biophys Res Commun. 2003 Aug 22;308(2):313-9. doi: 10.1016/s0006-291x(03)01380-9.

Abstract

Myelin basic protein (MBP) has been shown to bind calmodulin (CaM) in a specific Ca(2+)-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 alpha-helix.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites / genetics
  • Calmodulin / metabolism*
  • In Vitro Techniques
  • Kinetics
  • Mice
  • Molecular Sequence Data
  • Myelin Basic Protein / chemistry*
  • Myelin Basic Protein / genetics
  • Myelin Basic Protein / metabolism*
  • Protein Binding
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Deletion
  • Spectrometry, Fluorescence
  • Spectrometry, Mass, Electrospray Ionization
  • Tryptophan / chemistry

Substances

  • Calmodulin
  • Myelin Basic Protein
  • Recombinant Proteins
  • Tryptophan