Abstract
The molecular details of the formation of the myelin sheath, a multilayered membrane in the nervous system, are to a large extent unknown. P2 is a peripheral membrane protein from peripheral nervous system myelin, which is believed to play a role in this process. X-ray crystallographic studies and complementary experiments have provided information on the structure-function relationships in P2. In this study, a fully deuterated sample of human P2 was produced. Crystals that were large enough for neutron diffraction were grown by a ten-month procedure of feeding, and neutron diffraction data were collected to a resolution of 2.4 Å from a crystal of 0.09 mm(3) in volume. The neutron crystal structure will allow the positions of H atoms in P2 and its fatty-acid ligand to be visualized, as well as shedding light on the fine details of the hydrogen-bonding networks within the P2 ligand-binding cavity.
| Original language | English |
|---|---|
| Journal | Acta crystallographica. Section F, Structural biology communications |
| Volume | 71 |
| Issue number | Pt 11 |
| Pages (from-to) | 1391-5 |
| Number of pages | 5 |
| ISSN | 2053-230X |
| DOIs | |
| Publication status | Published - Nov 2015 |
Keywords
- Amino Acid Sequence
- Crystallization
- Humans
- Molecular Sequence Data
- Myelin P2 Protein/biosynthesis
- Myelin Sheath/genetics
- Neutron Diffraction/methods