%0 Journal Article %1 opella_structures_1999 %A Opella, S J %A Marassi, F M %A Gesell, J J %A Valente, A P %A Kim, Y %A Oblatt-Montal, M %A Montal, M %D 1999 %J Nat. Struct. Biol. %K Acid Amino Channel Channels,Isotope Conformation,Receptors,Recombinant Data,N-Methyl-D-Aspartate,Nicotinic,Peptide Fragments,Protein Gating,Ion Labeling,Lipid Proteins,Solutions Resonance Sequence Sequence,Chemical,Escherichia Spectroscopy,Micelles,Models,Molecular,Molecular bilayers,Lipids,Magnetic coli,Ion %N 4 %P 374--379 %R 10.1038/7610 %T Structures of the \M\2 channel-lining segments from nicotinic acetylcholine and \NMDA\ receptors by \NMR\ spectroscopy %V 6 %X 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.

@article{opella_structures_1999, abstract = {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.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Opella, S J and Marassi, F M and Gesell, J J and Valente, A P and Kim, Y and Oblatt-Montal, M and Montal, M}, biburl = {https://www.bibsonomy.org/bibtex/2b45866c7a904f4017b472ae89557c994/nmrresource}, doi = {10.1038/7610}, interhash = {d654bc920cf17e68227124f00d312b2e}, intrahash = {b45866c7a904f4017b472ae89557c994}, issn = {1072-8368}, journal = {Nat. Struct. Biol.}, keywords = {Acid Amino Channel Channels,Isotope Conformation,Receptors,Recombinant Data,N-Methyl-D-Aspartate,Nicotinic,Peptide Fragments,Protein Gating,Ion Labeling,Lipid Proteins,Solutions Resonance Sequence Sequence,Chemical,Escherichia Spectroscopy,Micelles,Models,Molecular,Molecular bilayers,Lipids,Magnetic coli,Ion}, month = apr, number = 4, pages = {374--379}, pmid = {10201407}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Structures of the {\{}M{\}}2 channel-lining segments from nicotinic acetylcholine and {\{}NMDA{\}} receptors by {\{}NMR{\}} spectroscopy}}, volume = 6, year = 1999 }