| General information | | DisProt: | DP00663 | | Name: | Myelin basic protein | | Synonym(s): | MBP_PIG
MBP
| | First appeared in release: | Release 5.6 (01/10/2011) | | UniProt: | P81558 | | UniGene: | | | SwissProt: | MBP_PIG | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Sus scrofa (Pig) | | Sequence length: | 171 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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ASQKRPSQRH GSKYLASAST MDHARHGFLP RHRDTGIDSL GRFFGADRGA PKRGSGKDGH - 60
HAARTTHYGS LPQKAQHGRP QDENPVVHFF KNIVTPRTPP PSQGKGRGLS LSRFSWGAEG - 120
QKPGFGYGGR APDYKPAHKG LKGAQDAQGT LSKIFKLGGR DSRSGSPMAR R
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| Functional narrative |
Myelin Basic Protein (MBP) is, along with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane. (UniProt)
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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 - 171 | | Length: | 171 | | Region sequence: |
ASQKRPSQRHGSKYLASASTMDHARHGFLPRHRDTGIDSLGRFFGADRGAPKRGSGKDGH
HAARTTHYGSLPQKAQHGRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEG
QKPGFGYGGRAPDYKPAHKGLKGAQDAQGTLSKIFKLGGRDSRSGSPMARR | | Modification type: | Complex
Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | | | Functional subclasses: | Substrate/ligand binding
Protein-protein binding
| Detection methods:
- Synchrotron radiation circular dichroism (SRCD) (pH: 7.6; CaCl2 2 mM; CaM (0.9 mg/mL; also pMBP:CaM complex 1:1, 1:2 ratios); KPO4 10 mM; pMBP (0.6 mg/mL; also in complex w/CaM 1:1, 1:2 ratios))
- Synchrotron radiation circular dichroism (SRCD) (pH: 7.6; KPO4 10 mM; pMBP; Zinc acetate (concentration range: 0.5 - 4 mM))
| References:
- Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgartel P, Heape AM, Lubec G, Kursula P. "Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule." Amino Acids. 2009. PubMed: 19855925
| Comments:Majava et al (2010) found that with pig myelin basic protein (pMBP) in complex with Calmodulin (CaM), pMBP did not gain significant structure. However, in the presence of high concentration of zinc, pMBP showed possible induced folding.
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| References |
- Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgartel P, Heape AM, Lubec G, Kursula P. "Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule." Amino Acids. 2009. PubMed: 19855925
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| Comments |
Sent for AV 1-12-2011 (PubMed: 19855925)
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