ArticleActa crystallographica. Section F, Structural biology communications2015
Production, crystallization and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Human Peripheral Myelin Protein 2 and Charcot-Marie-Tooth Disease or Structural Missense Variants Show Different Binding to Myelin-Like Lipid Monolayers.Chembiochem : a European journal of chemical biology · 2026Article
- Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice.The Journal of biological chemistry · 2020Article
- Sub-Atomic Resolution Crystal Structures Reveal Conserved Geometric Outliers at Functional Sites.Molecules (Basel, Switzerland) · 2019Article
- Molecular mechanisms of Charcot-Marie-Tooth neuropathy linked to mutations in human myelin protein P2.Scientific reports · 2017Article
- Back-exchange of deuterium in neutron crystallography: characterization by IR spectroscopy.Journal of applied crystallography · 2017Article
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6 authors.
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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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