Cytoplasmic domain of human myelin protein zero likely folded as beta-structure in compact myelin.

ABSTRACT: Myelin protein zero (P0 or P0 glycoprotein), the major integral membrane protein in peripheral nervous system myelin, plays a key role in myelin membrane compaction and stability. While the structure of P0 extracellular domain was determined by crystallography, the paucity of any structural data on the highly positive-charged P0 cytoplasmic domain (P0-cyt) has greatly limited our understanding of the mechanism of P0 function. Here, using circular dichroism and intrinsic fluorescence spectroscopy, we attempted to elucidate the structure of human P0-cyt (hP0-cyt) in membrane mimetic environments composed of detergents or lipid vesicles. We found that the secondary structure of P0-cyt was polymorphic-at the lipid/protein ratio corresponding to that of mature peripheral myelin ( approximately

SUBMITTER: Luo X 

PROVIDER: S-EPMC1796833 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature