ArticleActa crystallographica. Section D, Biological crystallography2014
Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 53 citations in OpenAlex.
- Identification of suicide brain transcriptomic signatures using meta-analysis of multiple cohorts.Translational psychiatry · 2026Pooled it
- Sorting of lysosomal enzyme and autophagy are regulated by the GGA1-induced TGN lipid scrambling.Science advances · 2026Article
- 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
- On the synergy between myelin proteins P0, MBP, and P2 in peripheral nerve major dense line formation.The FEBS journal · 2025Article
- Article
- Mechanical Responses of a Single Myelin Layer: A Molecular Simulation Study.Biomolecules · 2023Article
- Application of Computational Biology and Artificial Intelligence in Drug Design.International journal of molecular sciences · 2022Review
- A Role for Fatty Acids in Peripheral Neuropathy Associated with Type 2 Diabetes and Prediabetes.Antioxidants & redox signaling · 2022Review
- Human myelin proteolipid protein structure and lipid bilayer stacking.Cellular and molecular life sciences : CMLS · 2022Article
- How Does Protein Zero Assemble Compact Myelin?Cells · 2020Article
- 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
- A myelin sheath protein forming its lattice.The Journal of biological chemistry · 2020Article
- Review
- Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease.Cells · 2020Review
- Sub-Atomic Resolution Crystal Structures Reveal Conserved Geometric Outliers at Functional Sites.Molecules (Basel, Switzerland) · 2019Article
- Peripheral myelin protein 2 - a novel cluster of mutations causing Charcot-Marie-Tooth neuropathy.Orphanet journal of rare diseases · 2019Article
- Neuropathy-related mutations alter the membrane binding properties of the human myelin protein P0 cytoplasmic tail.PloS one · 2019Article
- 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
- The Role of Peripheral Myelin Protein 2 in Remyelination.Cellular and molecular neurobiology · 2018Article
- Molecular mechanisms of Charcot-Marie-Tooth neuropathy linked to mutations in human myelin protein P2.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.93 Å allows detailed structural analyses, including the full organization of an internal hydrogen-bonding network. The orientation of the bound fatty-acid carboxyl group is linked to the protonation states of two coordinating arginine residues. An anion-binding site in the portal region is suggested to be relevant for membrane interactions and conformational changes. When bound to membrane multilayers, P2 has a preferred orientation and is stabilized, and the repeat distance indicates a single layer of P2 between membranes. Simulations show the formation of a double bilayer in the presence of P2, and in cultured cells wild-type P2 induces membrane-domain formation. Here, the most accurate structural and functional view to date on P2, a major component of peripheral nerve myelin, is presented, showing how it can interact with two membranes simultaneously while going through conformational changes at its portal region enabling ligand transfer.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.