ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- 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
- Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins.BMC structural biology · 2018Article
- Molecular mechanisms of Charcot-Marie-Tooth neuropathy linked to mutations in human myelin protein P2.Scientific reports · 2017Article
- Production, crystallization and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Article
- Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.Acta crystallographica. Section D, Biological crystallography · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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