Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure.

ABSTRACT:

Background

The myelin sheath is a multilamellar membrane structure wrapped around the axon, enabling the saltatory conduction of nerve impulses in vertebrates. Myelin basic protein, one of the most abundant myelin-specific proteins, is an intrinsically disordered protein that has been shown to bind calmodulin. In this study, we focus on a 19-mer synthetic peptide from the predicted calmodulin-binding segment near the C-terminus of human myelin basic protein.

Results

The interaction of native human myelin basic protein with calmodulin was confirmed by affinity chromatography. The binding of the myelin basic protein peptide to calmodulin was tested with isothermal titration calorimetry (ITC) in different temperatures, and Kd was observed to be in the low muM range, as previous

SUBMITTER: Majava V 

PROVIDER: S-EPMC2288786 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature