| General information | | DisProt: | DP00237 | | Name: | Myelin basic protein | | Synonym(s): | MBP_MOUSE
MBP
Myelin A1 protein
| | First appeared in release: | Release 2.2 (04/14/2005) | | UniProt: | P04370 | | UniGene: | Mm.252063 | | SwissProt: | MBP_MOUSE | | TrEMBL: | | | NCBI (GI): | 17378829 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 169 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKDSH - 60
TRTTHYGSLP QKSQHGRTQD ENPVVHFFKN IVTPRTPPPS QGKGRGLSLS RFSWGAEGQK - 120
PGFGYGGRAS DYKSAHKGFK GAYDAQGTLS 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 | | Name: | | | Location: | 1 - 169 | | Length: | 169 | | Region sequence: |
MASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSH
TRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQK
PGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR | | Modification type: | Engineered
Isoform
Mutant
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
| References:
- Hill CM, Bates IR, White GF, Hallett FR, Harauz G. "Effects of the osmolyte trimethylamine-N-oxide on conformation, self-association, and two-dimensional crystallization of myelin basic protein." J Struct Biol. 2002; 139(1): 13-26. PubMed: 12372316
| Comments:The experimental sequence was the 18.5 kDa isoform.
The experimental sequence had a C-terminal hexahistidine tagged.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 33 - 46 | | Length: | 14 | | Region sequence: | |
| Modification type: | | | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | | Detection methods:
| References:
- Libich DS, Harauz G. "Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site." Biophys J. 2008; 94(12): 4847-66. PubMed: 18326633
| Comments:
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| References |
- Baran C, Smith GS, Bamm VV, Harauz G, Lee JS. "Divalent cations induce a compaction of intrinsically disordered myelin basic protein." Biochem Biophys Res Commun. 2010; 391(1): 224-9. PubMed: 19903451
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| Comments |
Additional UniGene IDs: Mm.392350 and Mm.454459
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