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| MAJOR MYELIN PROTEOLIPID - THE 4-ALPHA-HELIX TOPOLOGY |
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| Author(s): POPOT JL, DINH DP, DAUTIGNY A |
| Source: JOURNAL OF MEMBRANE BIOLOGY Volume: 120 Issue: 3 Pages: 233-246 Published: MAR 1991 |
| Times Cited: 117 References: 85 |
| Abstract: 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 alpha-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. |
| Document Type: Article |
| Language: English |
| Reprint Address: POPOT, JL (reprint author), CNRS, URA 1187, INST BIOL PHYS CHIM, F-75005 PARIS, FRANCE |
Addresses:
1. CNRS, URA 1187, COLL FRANCE, F-75005 PARIS, FRANCE |
| Publisher: SPRINGER VERLAG, 175 FIFTH AVE, NEW YORK, NY 10010 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology; Physiology |
| IDS Number: FD454 |
| ISSN: 0022-2631 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |