Extracellular domain of myelin oligodendrocyte glycoprotein (MOG) exhibits solvent-dependent conformational transitions.
The conformation of the non-glycosylated recombinant form of the extracellar domain of rat MOG (rMOG(1-125)) dissolved in different solvent conditions was studied by CD spectroscopy. The results show that rMOG(1-125) exhibits a predominantly beta sheet conformation in aqueous buffer solution at pH 7.5 and that this 'beta-form' is stabilized by zwitterionic phospholipids, DPC and LPCP. The alpha helical content of the protein can increase from 9% to up to 20% when TFE or anionic detergent LPAP and SDS are added.
Ngu-Schwemlein
Maria
M
Department of Chemistry, University of South Alabama, Mobile, AL 36688, USA.
Corzett
Michele
M
Thornton
Kevin H
KH
Balhorn
Rod
R
Cosman
Monique
M
D000818:Animals; D002942:Circular Dichroism; D005110:Extracellular Space / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008246:Lysophospholipids / Q000737:chemistry; D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein / Q000737:chemistry* / Q000378:metabolism; D063308:Myelin-Oligodendrocyte Glycoprotein; D009836:Oligodendroglia / Q000737:chemistry*; D010767:Phosphorylcholine / Q000031:analogs & derivatives* / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D051381:Rats; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D012997:Solvents / Q000737:chemistry*; D013696:Temperature; D014270:Trifluoroethanol / Q000737:chemistry
D008246:Lysophospholipids; C571328:Mog protein, rat; D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein; D063308:Myelin-Oligodendrocyte Glycoprotein; D012997:Solvents; D010767:Phosphorylcholine; D012967:Sodium Dodecyl Sulfate; C028810:dodecylphosphocholine; D014270:Trifluoroethanol; C032881:lysophosphatidic acid