Spatial structure of the M3 transmembrane segment of tire nicotinic acetylcholine receptor α subunit

European Journal of Biochemistry

Volumn 255, Issue 2, 1998, Pages 455-461

  Lugovskoy, Alexey A ^a   Maslennikov, Innokenty V ^a   Utkin, Yuri N ^a   Tsetlin, Victor I ^a   Cohen, Jonathan B ^b   Arseniev, Alexander S ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Conformational analysis; Membrane domain; Nicotinic acetylcholine receptor; NMR

Indexed keywords

NICOTINIC RECEPTOR; RECEPTOR SUBUNIT;

ARTICLE; INFRARED SPECTROPHOTOMETRY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; TORPEDO CALIFORNICA;

AMINO ACID SEQUENCE; ANIMALS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, NICOTINIC; TORPEDO;

EID: 0032527758     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550455.x     Document Type: Article

References (47)

1. Karlin, A. & Akabas, M. H. (1995) Toward a structural basis for the function of nicotinic acelylcholine receptors and their cousins. Neuron 15, 1231-1244.
2. Gazli, J.-L. & Changeux, J.-P. (1994) Neurotransmitter-gated ion channels as unconventional allosteric proteins, Curr. Opin. Struct. Biol. 4, 554-565.
3. Hucho, F., Tsetlin, V. I. & Machold, J. (1996) The emerging three-dimensional structure of a receptor. The nicotinic acetylcholine receptor, Eur. J. Biochem. 239, 539-557.
4. Akabas, M. H. & Karlin, A. (1995) Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α-subunit. Biochemistry 34, 12496-12500.
5. DiPaola, M., Kao, P. & Karlin, A. (1990) Mapping the α-subunit site photolaheled by the noncompetitive inhibitor [3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor, J. Biol Chem. 265, 11017-110129.
6. Montal, M. (1995) Design of molecular function: channels of communication, Annu. Rev. Biophys, Biomol. Struct. 24, 31-57.
7. Opella, S. J., Gessel, J., Valente, A. P., Marassi. F. M., Oblatt-Montal, M., Sun. W., Ferrer-Montiel, A. & Montal, M. (1997) Structural studies of the pore-lining segments of neurotransmitter-gated channels, Chemtracts - biochemistry and molecular biology 10, 153-174.
8. Giraudat, J., Montecucco, C., Bisson, R. & Changeux, J.-P. (1985) Transmembrane topology of acetylcholine receptor subunits probed with photoreactive phospholipids. Biochemistry 24, 3121-3127.
9. Blanton, M. P. & Cohen, J. B. (1994) Identifying the lipid-protein interface of the Torpedo nicotinic acelylcholine receptor: secondary structure implications, Biochemistry 33, 2859-2872.
10. Lee, Y. H., Li, L., Lasalde, J., Rojas, L., McNamee, M., Ortiz-Miranda, S. I. & Pappone, P. (1994) Mutations in the M4 domain of Torpedo californica acetylcholine receptor dramatically alter ion channel function, Biophys. J. 66, 646-653.
11. Lasalde, J. A., Tamamizu, S., Butler, D. H., Vibat, C. R., Hung, B. & McNamee, M. G. (1996) Tryptophan substitutions at the lipid-exposed transmembrane segment M4 of Torpedo californica acetylcholine receptor govern channel gating, Biochemistry 35, 14139-14148.
12. Unwin, N. (1993) Nicotinic acetylcholine receptor at 9 Å resolution, J. Mol. Biol. 229, 1101-1124.
13. White, B. H. & Cohen, J. B. (1992) Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist, J. Biol. Chem. 267, 15770-15783.
14. Akabas, M. H., Kaufmann, C., Archdeacon, P. & Karlin, A. (1994) Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit, Neuron 13, 919-927.
15. Blanton, M. P. & Cohen, J. B. (1992) Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor. Biochemistry 31, 3738-3750.
16. Arseniev, A. S., Kuryatov, A. B., Tsetlin, V. I., Bystrov, V. F., Ivanov, V. T. & Ovchinnikov, Yu. A. (1987) 19F NMR study of 5-fluorotryptophan-labeled bacteriorhodopsin, FEBS Lett. 213, 283-288.
17. 1H NMR spectroscopy. Bioorg. Khim. 21, 659-674.
18. Maslennikov, I. V., Lugovskoi, A. A., Arseniev, A. S., Chikin, L. D. & Ivanov, V. T. (1997) The spatial structure of the 87-136 bacterioopsin fragment, Bioorg. Khim. 23, 771-782.
19. 15N NMR spectroscopy. J. Biomol. NMR. 6, 113-122.
20. 1H heteronuclear NMR spectroscopy, Eur. J. Biochem. 219, 571-583.
21. Schuldiner, S., Lebendiker, M. & Yerushalmi, H. (1997) EmrE, the smallest ion-coupled transporter, provides a unique paradigm for structure-function studies, J. Exp. Biol. 200, 335-341.
22. Gratias, R. & Kessler, H. (1997) Molecular dynamics study of microheterogeneity and preferential solvation in methanol/chloroform mixtures, J. Phys. Chem. B. in the press.
23. Gorne-Tschelnokow, U., Strecker, A., Kaduk, C., Naumann, D. & Hucho, F. (1994) The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β structures, EMBO J. 13, 338-341.
24. Baenziger, J. E. & Methot, N. (1995) Fourier transform infrared and hydrogen/deuterium exchange reveal an exchange-resistant core of α-helical peptide hydrogens in the nicotinic acetylcholine receptor, J. Biol. Chem 270, 29129-29137.
25. 1H-NMR spectra of protein via double quantum filter. Biochem. Biophys. Res. Commun. 117, 479-485.
26. Bax. A. & Davis, D. G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-366.
27. Jeener, J., Meier, G. H., Bachman, P. & Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4553.
28. States, D. J., Habercorn, R. A. & Ruben, D. J. (1982) 2D NOE with pure absorption phase in four quadrants, J. Magn. Reson. 48, 286-292.
29. Piotto, M., Saudek, V. & Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665.
30. Lippens, G., Dhalluin, C. & Wieruszeski, J.-M. (1995) Use of a water flip-back pulse in the homonuclear NOESY experiment. J. Biomol. NMR 5, 327-331.
31. Bartels, C., Xia, T.-h., Billeter, M., Guntert, P. & Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR 6, 1-10.
32. Wüthrich. K. (1986) NMR of proteins and nucleic acids, John Wiley & Sons, NY.
33. Guntert, P., Braun, W. & Wüthrich, K. (1991) Efficient computation of 3D protein structures in solution from NMR data using the program DIANA and supporting programs CALIBA, HABAS and GLOMSA, J. Mol Biol. 217, 517-530.
34. Szypersky, T., Guntert, P., Otting, G. & Wüthrich, K. (1992) Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets, J. Magn. Reson. 99, 552-560.
35. Nemethy, G., Pottle, M. S. & Sheraga, H. A. (1983) Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions and hydrogen bond interactions for the naturally occurring amino acids. J. Phys. Chem. 87, 1883-1887.
36. Schaumann, T., Braun, W. & Wüthrich, K. (1990) The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space. Biopolymers 29, 679-694.
37. Borgias, B. A. & James, T. L. (1990) MARDIGRAS - a procedure for matrix analysis of relaxation for peptide geometry of an aqueous structure, J. Magn. Reson. 87, 475-487.
38. Keepers, J. W. & James, T. L. (1984) A theoretical study of distance determinations from NMR. Two dimensional nuclear Overhauser effects spectra, J. Magn Reson. 57, 404-426.
39. Baker, E. N. & Hubburd, R. E. (1984) Hydrogen bonding in globular proteins. Prog. Biophys. Mol Biol. 44, 97-179.
40. Koradi, R., Billeter, M. & Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55.
41. 10-Helices in peptides and proteins as studied by modified Zimm-Bragg theory, J. Am. Chem. Soc. 117, 10098-10103.
42. Barsukov, I. L., Nolde, D. E., Lomize, A. L. & Arseniev, A. S. (1992) Three-dimensional structure of proteolytic fragment 163-231 of bacterioopsin determined from nuclear magnetic resonance data in solution. Eur: J. Biochem. 206, 665-672.
43. Henderson, R. & Unwin, P. N. T. (1975) Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257, 28-32.
44. Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M. & Henderson. R. (1996) Electron-crystallographic refinement of the structure of bacteriorhodopsin, J. Mol. Biol. 259, 393-421.
45. 15N NMR relaxation: Analysis of dynamic models of one- and two-helical subunits of bacterioopsin, J. Biomol. NMR. 5, 383-396.
46. 15N-NMR studies of bacteriorhodopsin Halobacterium halobium. Conformational dynamics of the four-helical bundle. Eur. J. Biochem. 210, 223-229.
47. Li, S. C., Kim, P. K. & Deber, C. M. (1995) Manipulation of peptide conformations by fine-tuning of the environment and/or the primary sequence. Biopolymers 35, 667-675.