Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule

@article{Majava2009StructuralAO,
  title={Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule},
  author={Viivi Majava and Chaozhan Wang and Matti Myllykoski and Salla M. Kangas and Sung Ung Kang and Nobuhiro Hayashi and Peter Baumg{\"a}rtel and Anthony M. Heape and Gert Lubec and Petri Kursula},
  journal={Amino Acids},
  year={2009},
  volume={39},
  pages={59-71}
}
Myelin basic protein (MBP) is present between the cytoplasmic leaflets of the compact myelin membrane in both the peripheral and central nervous systems, and characterized to be intrinsically disordered in solution. One of the best-characterized protein ligands for MBP is calmodulin (CaM), a highly acidic calcium sensor. We pulled down MBP from human brain white matter as the major calcium-dependent CaM-binding protein. We then used full-length brain MBP, and a peptide from rodent MBP, to… CONTINUE READING
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