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The current status of structural studies on proteins of the myelin sheath (Review) Kursula PInt J Mol Med 2001[Nov]; 8 (5): 475-9Myelin, 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.|2',3'-Cyclic-Nucleotide Phosphodiesterases/chemistry[MESH]|Animals[MESH]|Humans[MESH]|Models, Molecular[MESH]|Myelin Basic Protein/chemistry[MESH]|Myelin P0 Protein/chemistry[MESH]|Myelin P2 Protein/chemistry[MESH]|Myelin Proteins/*chemistry[MESH]|Myelin Sheath/*chemistry[MESH]|Myelin-Associated Glycoprotein/chemistry[MESH]|Protein Conformation[MESH] |
