The encephalitogenic protein of myelin forms hexamers in which the polypeptides have a pleated‐sheet structure

FEBS Letters

Smith, Ross¹ 

[1] Department of Biochemistry, University of Queensland, St. Lucia, QLD 4067, Australia

关键词: Myelin;    Basic protein;    Protein self-association;    Circular dichroism;    β-pleated sheet;    Lysophosphatidylcholine;    MBP;    myelin basic protein;    lyso PC;    myristoyllysophosphatidylcholine;    CD;    circular dichroism;   

DOI  :  10.1016/0014-5793(85)80804-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sedimentation equilibrium data are shown to be consistent with the existence in solution of an equilibrium between monomers and hexamers of bovine myelin basic protein, without significant accumulation of intermediates. At low concentrations circular dichroism spectra were indicative of an aperiodic coiled secondary structure. At higher concentrations, where the protein self-associates, they showed formation of a β-pleated sheet conformation. At low molar ratios myristoyllysophosphatidylcholine promotes protein self-association and the concomitant conformational transition. The data are consistent with the existence of an equilibrium mixture of relatively unstructured monomers and hexamers in which the polypeptides have a welldefined three-dimensional structure.

【 授权许可】

Unknown