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== Structure == |
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Myelin basic protein is a net-positive, membrane-associated, intrinsically disordered protein. It is basic, with an isoelectric point of 10, and is thought to associate with negatively charged phospholipid heads of the plasma membrane. Due to post-translational modifications, it can exist as various charge isomers known as C1-C6 or C8. C1-C6 each undergo ADP-ribosylation at Arg9 and Arg54; in addition, C1 is the least modified (and most positively charged), C2 is deamidated, and C3-C6 undergo a combination of phosphorylation, deamidation, and deimination. C8 is the most distinct, containing 6-11 citrullinations beyond C1, each of which decrease its positive charge and alter its ability to hydrogen bond. Additionally, they may undergo acylation of the N-terminal alanine, methylation of Arg107, and addition of an azido-GTP at Gln3.<ref>{{Cite journal|last=Boggs|first=J. M.|date=2006-06-23|title=Myelin basic protein: a multifunctional protein|url=http://dx.doi.org/10.1007/s00018-006-6094-7|journal=Cellular and Molecular Life Sciences|volume=63|issue=17|pages=1945–1961|doi=10.1007/s00018-006-6094-7|issn=1420-682X}}</ref> |
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Myelin basic protein has been classified as an intrinsically disordered protein that has no stable secondary structure in solution.<ref>{{Cite journal|last=Anderson|first=T. R.|last2=Slotkin|first2=T. A.|date=1975-08-15|title=Maturation of the adrenal medulla--IV. Effects of morphine|url=https://pubmed.ncbi.nlm.nih.gov/7|journal=Biochemical Pharmacology|volume=24|issue=16|pages=1469–1474|doi=10.1016/0006-2952(75)90020-9|issn=1873-2968|pmid=7}}</ref> Like most IDPs, it has a high net charge and a low mean hydrophobicity, minimizing the hydrophobic effect that drives traditional protein folding. It does contain some exceptions to normal IDP amino acid content. For example, MBP has more arginine and less glutamic acid than most IDPs. However, this is likely because those changes are necessary for MBP to be sufficiently basic and positively charged to correctly interact with the membrane.<ref>{{Cite journal|last=HARAUZ|first=G|date=2004-05|title=Myelin basic protein?diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis|url=http://dx.doi.org/10.1016/s0968-4328(04)00096-4|journal=Micron|doi=10.1016/s0968-4328(04)00096-4|issn=0968-4328}}</ref> Notably, MBP has been shown to adopt a more stable secondary structure on interaction with lipids.<ref>{{Cite journal|last=Moroi|first=K.|last2=Sato|first2=T.|date=1975-08-15|title=Comparison between procaine and isocarboxazid metabolism in vitro by a liver microsomal amidase-esterase|url=https://pubmed.ncbi.nlm.nih.gov/8|journal=Biochemical Pharmacology|volume=24|issue=16|pages=1517–1521|doi=10.1016/0006-2952(75)90029-5|issn=1873-2968|pmid=8}}</ref><ref>{{Cite journal|last=Marniemi|first=J.|last2=Parkki|first2=M. G.|date=1975-09-01|title=Radiochemical assay of glutathione S-epoxide transferase and its enhancement by phenobarbital in rat liver in vivo|url=https://pubmed.ncbi.nlm.nih.gov/9|journal=Biochemical Pharmacology|volume=24|issue=17|pages=1569–1572|doi=10.1016/0006-2952(75)90080-5|issn=0006-2952|pmid=9}}</ref> Experiments have predicted this structure to contain beta sheet and regions of amphipathic helix. |
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Latest revision as of 16:18, 24 November 2020
Structure
[edit]Myelin basic protein is a net-positive, membrane-associated, intrinsically disordered protein. It is basic, with an isoelectric point of 10, and is thought to associate with negatively charged phospholipid heads of the plasma membrane. Due to post-translational modifications, it can exist as various charge isomers known as C1-C6 or C8. C1-C6 each undergo ADP-ribosylation at Arg9 and Arg54; in addition, C1 is the least modified (and most positively charged), C2 is deamidated, and C3-C6 undergo a combination of phosphorylation, deamidation, and deimination. C8 is the most distinct, containing 6-11 citrullinations beyond C1, each of which decrease its positive charge and alter its ability to hydrogen bond. Additionally, they may undergo acylation of the N-terminal alanine, methylation of Arg107, and addition of an azido-GTP at Gln3.[1]
Myelin basic protein has been classified as an intrinsically disordered protein that has no stable secondary structure in solution.[2] Like most IDPs, it has a high net charge and a low mean hydrophobicity, minimizing the hydrophobic effect that drives traditional protein folding. It does contain some exceptions to normal IDP amino acid content. For example, MBP has more arginine and less glutamic acid than most IDPs. However, this is likely because those changes are necessary for MBP to be sufficiently basic and positively charged to correctly interact with the membrane.[3] Notably, MBP has been shown to adopt a more stable secondary structure on interaction with lipids.[4][5] Experiments have predicted this structure to contain beta sheet and regions of amphipathic helix.
References:
1. Ahmed et al. “Induced Secondary Structure and Polymorphism in an Intrinsically
Disordered Structural Linker of the CNS: Solid-State NMR and FTIR
Spectroscopy of Myelin Basic Protein Bound to Actin.”
2. Radivojac, P., L. M. Iakoucheva, C. J. Oldfield, Z. Obradovic, V. N.
Uversky, et al. 2007. Intrinsic disorder and functional proteomics.
Biophys. J. 92:1439–1456. (IDPs)
3. Receveur-Brechot, V., J. M. Bourhis, V. N. Uversky, B. Canard, and S.
Longhi. 2006. Assessing protein disorder and induced folding. Proteins.
62:24–45. (IDPs)
4. Boggs, J. M. 2006. Myelin basic protein: a multifunctional protein. Cell.
Mol. Life Sci. 63:1945–1961. (Review)
5. Boggs, J. M., G. Rangaraj, W. Gao, and Y. M. Heng. 2006. Effect of
phosphorylation of myelin basic protein by MAPK on its interactions
with actin and actin binding to a lipid membrane in vitro. Biochemistry.
45:391–401.
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- ^ Boggs, J. M. (2006-06-23). "Myelin basic protein: a multifunctional protein". Cellular and Molecular Life Sciences. 63 (17): 1945–1961. doi:10.1007/s00018-006-6094-7. ISSN 1420-682X.
- ^ Anderson, T. R.; Slotkin, T. A. (1975-08-15). "Maturation of the adrenal medulla--IV. Effects of morphine". Biochemical Pharmacology. 24 (16): 1469–1474. doi:10.1016/0006-2952(75)90020-9. ISSN 1873-2968. PMID 7.
- ^ HARAUZ, G (2004-05). "Myelin basic protein?diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis". Micron. doi:10.1016/s0968-4328(04)00096-4. ISSN 0968-4328.
{{cite journal}}: Check date values in:|date=(help) - ^ Moroi, K.; Sato, T. (1975-08-15). "Comparison between procaine and isocarboxazid metabolism in vitro by a liver microsomal amidase-esterase". Biochemical Pharmacology. 24 (16): 1517–1521. doi:10.1016/0006-2952(75)90029-5. ISSN 1873-2968. PMID 8.
- ^ Marniemi, J.; Parkki, M. G. (1975-09-01). "Radiochemical assay of glutathione S-epoxide transferase and its enhancement by phenobarbital in rat liver in vivo". Biochemical Pharmacology. 24 (17): 1569–1572. doi:10.1016/0006-2952(75)90080-5. ISSN 0006-2952. PMID 9.