Abstract
The myelin sheath is a multilayered membrane that surrounds and insulates axons in the nervous system. One of the proteins specific to the peripheral nerve myelin is P2, a protein that is able to stack lipid bilayers. With the goal of obtaining detailed information on the structure-function relationship of P2, 14 structure-based mutated variants of human P2 were generated and produced. The mutants were designed to potentially affect the binding of lipid bilayers by P2. All mutated variants were also crystallized and preliminary crystallographic data are presented. The structural data from the mutants will be combined with diverse functional assays in order to elucidate the fine details of P2 function at the molecular level.
| Original language | English |
|---|---|
| Journal | Acta Crystallographica Section F: Structural Biology Communications |
| Volume | 68 |
| Issue number | Pt 11 |
| Pages (from-to) | 1359-62 |
| Number of pages | 4 |
| ISSN | 2053-230X |
| DOIs | |
| Publication status | Published - 1 Nov 2012 |
Keywords
- Amino Acid Substitution
- Crystallization
- Escherichia coli
- Humans
- Hydrophobic and Hydrophilic Interactions
- Models, Molecular
- Mutagenesis, Site-Directed
- Myelin P2 Protein/biosynthesis
- Protein Structure, Secondary
- Protein Structure, Tertiary
- X-Ray Diffraction