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Myelin basic protein (MBP) is the second most abundant protein in central nervous system myelin and is essential for maintaining the structure of the myelin sheath by promoting adhesion between cytosolic surfaces of multilayered compact myelin. It belongs to the intrinsically disordered or conformationally adaptable family of proteins, meaning it lacks a stable secondary structure in solution but can adopt more defined structures upon binding to lipids or other molecules. MBP interacts with various polyanionic proteins (e.g., actin, tubulin, Ca²⁺-calmodulin, clathrin) and negatively charged lipids. Some isoforms are transported into the nucleus and may bind polynucleotides. MBP is also involved in signaling within oligodendrocytes due to changes in phosphorylation triggered by extracellular signals[1][2][5].
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