The current status of structural studies on proteins of the myelin sheath (Review).
Myelin, the multilayered membrane structure surrounding axons, provides a unique environment to its proteins, which are either transmembrane proteins or interacting intimately with the membrane surface. Although myelin-specific proteins have been studied for decades, remarkably little is known of their three-dimensional structures. In addition, the exact functions of myelin proteins are to a large extent unknown. In this report, our current knowledge of peripheral nervous system myelin protein structures is reviewed, and the current status of attempts to solve the structures of full-length myelin proteins is evaluated. Furthermore, molecular models for the extracellular domain of the myelin-associated glycoprotein and the putative kinase-like domain of 2',3'-cyclic nucleotide 3'-phosphodiesterase are presented and discussed.
Kursula
P
P
Department of Biochemistry and Biocenter Oulu, University of Oulu, FIN-90014 Oulu, Finland. petri.kursula@oulu.fi
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000737:chemistry; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D004676:Myelin Basic Protein / Q000737:chemistry; D018993:Myelin P0 Protein / Q000737:chemistry; D018996:Myelin P2 Protein / Q000737:chemistry; D009185:Myelin Proteins / Q000737:chemistry*; D009186:Myelin Sheath / Q000737:chemistry*; D018992:Myelin-Associated Glycoprotein / Q000737:chemistry; D011487:Protein Conformation
D004676:Myelin Basic Protein; D018993:Myelin P0 Protein; D018996:Myelin P2 Protein; D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein; C073687:PMP22 protein, human; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases; C039809:2',3'-cyclic nucleotide 2'-phosphodiesterase