Publication: Conformational study on a myelin basic protein fragment: molecular dynamics simulations in membrane
All || By Area || By Year| Title | Conformational study on a myelin basic protein fragment: molecular dynamics simulations in membrane | Authors/Editors* | E. Polverini, G. Harauz |
|---|---|
| Where published* | EBSA 2009 - 7th European Biophysics Congress, Genoa, Italy |
| How published* | Proceedings |
| Year* | 2009 |
| Volume | 38 |
| Number | Supplement 1 |
| Pages | S38 |
| Publisher | European Biophysics Journal |
| Keywords | |
| Link | |
| Abstract |
Myelin basic protein (MBP) is a multifunctional protein of the central nervous system whose principal role is in maintaining the compactness and integrity of the myelin sheath, the multilamellar membrane wrapped around nerve axons. However, MBP also interacts with other proteins such as cytoskeletal and signalling proteins, adapting its structure to the different roles. MBP is a candidate autoantigen in the human demyelinating disease multiple sclerosis. This study investigated at atomic detail the conformation of a highly conserved central fragment of MBP, constisting of two consecutive regions with different relevant functionalities. The first one is associated with the membrane and comprises the primary immunodominant epitope in multiple sclerosis; the second one was predicted to be a ligand for SH3-domains of signalling proteins. Molecular dynamics simulations were perfomed in the presence of odecylphosphocholine micelle, starting from a structure extrapolated from experimental data (Harauz and Libich, Curr. Protein Pept. Sci., 2009). The results confirm the experimental hypothesis, showing, in the micelle, a stable alpha-helix anchored to the membrane for the first region and, for the proline-rich second one, a poly-proline type II helix pointing outwards, ready to interact with the signalling proteins. |
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