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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.


Saara Laulumaa, Matthew P Blakeley, Arne Raasakka, Martine Moulin, Michael Härtlein, Petri Kursula. Production, crystallization and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2. Acta crystallographica. Section F, Structural biology communications. 2015 Nov;71(Pt 11):1391-5

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PMID: 26527266

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