Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
| Autor: | S J, Opella, F M, Marassi, J J, Gesell, A P, Valente, Y, Kim, M, Oblatt-Montal, M, Montal |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Protein Conformation Lipid Bilayers Molecular Sequence Data Receptors Nicotinic Lipids Receptors N-Methyl-D-Aspartate Ion Channels Peptide Fragments Recombinant Proteins Article Solutions Models Chemical Isotope Labeling Escherichia coli Amino Acid Sequence Ion Channel Gating Micelles |
| Zdroj: | Nature structural biology. 6(4) |
| ISSN: | 1072-8368 |
| Popis: | The structures of functional peptides corresponding to the predicted channel-lining M2 segments of the nicotinic acetylcholine receptor (AChR) and of a glutamate receptor of the NMDA subtype (NMDAR) were determined using solution NMR experiments on micelle samples, and solid-state NMR experiments on bilayer samples. Both M2 segments form straight transmembrane alpha-helices with no kinks. The AChR M2 peptide inserts in the lipid bilayer at an angle of 12 degrees relative to the bilayer normal, with a rotation about the helix long axis such that the polar residues face the N-terminal side of the membrane, which is assigned to be intracellular. A model built from these solid-state NMR data, and assuming a symmetric pentameric arrangement of M2 helices, results in a funnel-like architecture for the channel, with the wide opening on the N-terminal intracellular side. |
| Databáze: | OpenAIRE |
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