The current status of structural studies on proteins of the myelin sheath (review)

Authors
Citation
P. Kursula, The current status of structural studies on proteins of the myelin sheath (review), INT J MOL M, 8(5), 2001, pp. 475-479
Citations number
53
Categorie Soggetti
Medical Research General Topics
Journal title
INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE
ISSN journal
11073756 → ACNP
Volume
8
Issue
5
Year of publication
2001
Pages
475 - 479
Database
ISI
SICI code
1107-3756(200111)8:5<475:TCSOSS>2.0.ZU;2-B
Abstract
Myelin, the multilayered membrane structure surrounding axons, provides a u nique environment to its proteins, which are either transmembrane proteins or interacting intimately with the membrane surface. Although myelin-specif ic proteins have been studied for decades, remarkably little is known of th eir three-dimensional structures. In addition, the exact functions of myeli n proteins are to a large extent unknown. In this report, our current knowl edge of peripheral nervous system myelin protein structures is reviewed, an d the current status of attempts to solve the structures of full-length mye lin proteins is evaluated. Furthermore, molecular models for the extracellu lar domain of the myelin-associated glycoprotein and the putative kinase-li ke domain of 2',3'-cyclic nucleotide T-phosphodiesterase are presented and discussed.