General information | DisProt: | DP00047 | Name: | Myelin basic protein | Synonym(s): | MBP_BOVIN
MBP
Myelin A1 protein
20 kDa microtubule stabilizing protein
| First appeared in release: | Release 1.0 (08/01/2003) | UniProt: | P02687 | UniGene: | Bt.64741 | SwissProt: | MBP_BOVIN | TrEMBL: | | NCBI (GI): | 126796 | Source organism: | Bos taurus (Bovine) | Sequence length: | 169 | Percent disordered: | 100% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP KRGSGKDGHH - 60 AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP SQGKGRGLSL SRFSWGAEGQ - 120 KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS KIFKLGGRDS RSGSPMARR
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Functional narrative |
Myelin basic protein (MBP) has a role in formation and stabilization of bilayers in the central and peripheral nervous system. MBP self associates as a homodimer on the cytoplasmic side of myelin. According to the CD spectra, lipid-free protein is mainly disordered with small amounts of alpha-helix and beta-sheet. The addition of lipid induces stabilization with secondary structure formation. There is an increase in alpha-helix and beta-sheet upon transition from a polar to an apolar environment.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered - Extended | Name: | | Location: | 1 - 169 | Length: | 169 | Region sequence: |
AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHH AARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQ KPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR | Modification type: | | PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Molecular assembly
| Functional subclasses: | Protein-lipid interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
| References:
- Polverini, E. Fasano, A. Zito, F. Riccio, P. Cavatorta, P. "Conformation of bovine myelin basic protein purified with bound lipids." Eur Biophys J. 1999; 28(4): 351-355. PubMed: 10394626
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