ArticleBiophysical journal2008
Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 55 citations in OpenAlex.
- On the synergy between myelin proteins P0, MBP, and P2 in peripheral nerve major dense line formation.The FEBS journal · 2025Article
- The intrinsically disordered protein glue of the myelin major dense line: Linking AlphaFold2 predictions to experimental data.Biochemistry and biophysics reports · 2023Article
- Variation of Structural and Dynamical Flexibility of Myelin Basic Protein in Response to Guanidinium Chloride.International journal of molecular sciences · 2022Article
- Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease.Cells · 2020Review
- The effect of DPP-4 inhibition to improve functional outcome after stroke is mediated by the SDF-1α/CXCR4 pathway.Cardiovascular diabetology · 2018Article
- Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins.Journal of biomolecular NMR · 2017Article
- Membrane Association Landscape of Myelin Basic Protein Portrays Formation of the Myelin Major Dense Line.Scientific reports · 2017Article
- Potential protein targets of the peptidylarginine deiminase 2 and peptidylarginine deiminase 4 enzymes in rheumatoid synovial tissue and its possible meaning.European journal of rheumatology · 2016Article
- The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro.Bioscience reports · 2014Article
- Interaction of myelin basic protein with cytoskeletal and signaling proteins in cultured primary oligodendrocytes and N19 oligodendroglial cells.BMC research notes · 2014Article
- The Stress-response protein prostate-associated gene 4, interacts with c-Jun and potentiates its transactivation.Biochimica et biophysica acta · 2014Article
- Myelin management by the 18.5-kDa and 21.5-kDa classic myelin basic protein isoforms.Journal of neurochemistry · 2013Review
- Article
- The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal.Biochemical and biophysical research communications · 2012Article
- Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytes.Journal of neuroscience research · 2012Article
- Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.Biochimica et biophysica acta · 2011Article
- Structured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interaction.Biophysical journal · 2011Article
- Charge isomers of myelin basic protein: structure and interactions with membranes, nucleotide analogues, and calmodulin.PloS one · 2011Article
- Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous system.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2010Review
- Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 18.5 kDa isoform of myelin basic protein (MBP) is the predominant form in adult human central nervous system myelin. It is an intrinsically disordered protein that functions both in membrane adhesion, and as a linker connecting the oligodendrocyte membrane to the underlying cytoskeleton; its specific interactions with calmodulin and SH3-domain containing proteins suggest further multifunctionality in signaling. Here, we have used multidimensional heteronuclear nuclear magnetic resonance spectroscopy to study the conformational dependence on environment of the protein in aqueous solution (100 mM KCl) and in a membrane-mimetic solvent (30% TFE-d(2)), particularly to analyze its secondary structure using chemical shift indexing, and to investigate its backbone dynamics using (15)N spin relaxation measurements. Collectively, the data revealed three major segments of the protein with a propensity toward alpha-helicity that was stabilized by membrane-mimetic conditions: T33-D46, V83-T92, and T142-L154 (murine 18.5 kDa sequence numbering). All of these regions corresponded with bioinformatics predictions of ordered secondary structure. The V83-T92 region comprises a primary immunodominant epitope that had previously been shown by site-directed spin labeling and electron paramagnetic resonance spectroscopy to be alpha-helical in membrane-reconstituted systems. The T142-L154 segment overlapped with a predicted calmodulin-binding site. Chemical shift perturbation experiments using labeled MBP and unlabeled calmodulin demonstrated a dramatic conformational change in MBP upon association of the two proteins, and were consistent with the C-terminal segment of MBP being the primary binding site for calmodulin.
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