The structural characteristics of myelin basic protein (MBP) involved in protein-protein and protein-lipid interactions were investigated. Rabbit MBP could bind calmodulin (CaM) in the presence of Ca2+ to form a complex that remained undissociated in 8 M urea. However, no tight complex formation was
โฆ LIBER โฆ
Myelin basic protein interacts with the myelin-specific ganglioside GM4
โ Scribed by Brian R. Mullin; Francis X. Decandis; Anthony J. Montanaro; John D. Reid
- Book ID
- 118867048
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 926 KB
- Volume
- 222
- Category
- Article
- ISSN
- 0006-8993
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The interaction of myelin basic protein with cholesterol and the conformational changes occurring in the protein upon interaction with the lipid were investigated. The myelin basic protein (MBP) plays an important role in stabilizing the multilamellar structure of the myelin membrane. MBP interacts