It plays an important role in the formation or maintenance of the multilamellar structure of myelin.
The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the efficiency of axonal impulse conduction.
[2] In humans, point mutations in PLP are the cause of Pelizaeus–Merzbacher disease (PMD), a neurologic disorder of myelin metabolism.
In animals demyelinating diseases such as mouse 'jimpy' or dog 'shaking pup' are also caused by mutations in PLP.
PLP is a highly conserved[3] hydrophobic protein of 276 to 280 amino acids which seems to contain four transmembrane segments, two disulfide bonds and which covalently binds lipids (at least six palmitate groups in mammals).