Production, crystallization and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2.
Acta Crystallogr F Struct Biol Commun
; 71(Pt 11): 1391-5, 2015 Nov.
Article
em En
| MEDLINE
| ID: mdl-26527266
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteína P2 de Mielina
/
Difração de Nêutrons
/
Bainha de Mielina
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article