Myelin proteolipid protein

Myelin proteolipid protein (PLP or lipophilin)
Identifiers
Symbol	Myelin_PLP
Pfam	PF01275
InterPro	IPR001614
SMART	SM00002
PROSITE	PDOC00497
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Myelin proteolipid protein (PLP or lipophilin) is the major myelin protein from the central nervous system (CNS). 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.

In man point mutations in PLP are the cause of Pelizaeus-Merzbacher disease (PMD), a neurologic disorder of myelin metabolism. In animals dismyelinating diseases such as mouse 'jimpy' or dog 'shaking pup' are also caused by mutations in PLP.

PLP is a highly conserved 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). PLP is highly related to GPM6A, a neuronal membrane glycoprotein.

Human proteins containing this domain

GPM6A; GPM6B; PLP1;

See also

• PLP2

References

This article incorporates text from the public domain Pfam and InterPro IPR001614