ISSN:
1432-1424
Keywords:
PLP
;
DM20
;
oligodendrocyte
;
myelin sheath
;
Pelizaeus-Merzbacher disease
;
dysmyelination
;
Jimpy mutation
;
integral membrane protein
;
transmembrane topology
;
hydrophobic α-helix
;
hydrophobicity analysis
;
model building
;
prediction
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Summary Several conflicting models have been proposed for the membrane arrangement of the major myelin proteolipid (PLP). We have compared features of the sequence of PLP with those of other eukaryotic integral membrane proteins, with the view of identifying the most likely transmembrane topology. A new, simple model is suggested, which features four hydrophobic α-helices spanning the whole thickness of the lipid bilayer. Its orientation may be such that both the N-and C-termini face the cytosol. None of the biochemical, biophysical or immunological experiments hitherto reported provides incontrovertible evidence against the model. The effect or absence thereof of various PLP mutations is discussed in the frame, of the proposed 4-helix topology.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01868534
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