Stereochemical issues in studies of ion channel proteins

Chirality

Volumn 10, Issue 1-2, 1998, Pages 8-13

  Dougherty, Dennis A ^a  

^a California Institute of Technology   (United States)

Author keywords

Ion channel proteins; K+ channels; nAChR; Stereochemistry; Subunit arrangement

Indexed keywords

ION CHANNEL; NICOTINIC RECEPTOR; POTASSIUM CHANNEL; PROTEIN SUBUNIT;

ARTICLE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STEREOCHEMISTRY;

EID: 0031906348     PISSN: 08990042     EISSN: None     Source Type: Journal    
DOI: 10.1002/chir.3     Document Type: Article

References (30)

1. For valuable general introductions to the field, see: Hall, Z.W., ed. An Introduction to Molecular Neurobiology. Sunderland, MA: Sinauer Associates, Inc., 1992; Hille, B. Ionic Channels of Excitable Membranes. Sunderland, MA: Sinauer Associates, Inc., 1992.
2. For valuable general introductions to the field, see: Hall, Z.W., ed. An Introduction to Molecular Neurobiology. Sunderland, MA: Sinauer Associates, Inc., 1992; Hille, B. Ionic Channels of Excitable Membranes. Sunderland, MA: Sinauer Associates, Inc., 1992.
3. For reviews of the nAChR, see: (a) Lester, H.A. The permeation pathway of neurotransmitter-gated ion channels. Annu. Rev. Biophys. Biomol. Struct. 21:267-292, 1992; (b) Karlin, A. Structure of nicotinic acetylcholine receptors. Curr. Opin. Neurobiol. 3:299-309, 1993; (c) Devillers-Thiéry, A., Galzi, J.L., Eiselé, J.L., Bertrand, S., Bertrand, D., Changeaux, J.P. Functional architecture of the nicotinic acetylcholine receptor: A prototype of ligand-gated ion channels. J. Membr. Biol. 136:97-112, 1993.
4. For reviews of the nAChR, see: (a) Lester, H.A. The permeation pathway of neurotransmitter-gated ion channels. Annu. Rev. Biophys. Biomol. Struct. 21:267-292, 1992; (b) Karlin, A. Structure of nicotinic acetylcholine receptors. Curr. Opin. Neurobiol. 3:299-309, 1993; (c) Devillers-Thiéry, A., Galzi, J.L., Eiselé, J.L., Bertrand, S., Bertrand, D., Changeaux, J.P. Functional architecture of the nicotinic acetylcholine receptor: A prototype of ligand-gated ion channels. J. Membr. Biol. 136:97-112, 1993.
5. For reviews of the nAChR, see: (a) Lester, H.A. The permeation pathway of neurotransmitter-gated ion channels. Annu. Rev. Biophys. Biomol. Struct. 21:267-292, 1992; (b) Karlin, A. Structure of nicotinic acetylcholine receptors. Curr. Opin. Neurobiol. 3:299-309, 1993; (c) Devillers-Thiéry, A., Galzi, J.L., Eiselé, J.L., Bertrand, S., Bertrand, D., Changeaux, J.P. Functional architecture of the nicotinic acetylcholine receptor: A prototype of ligand-gated ion channels. J. Membr. Biol. 136:97-112, 1993.
6. Unwin, N. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229:1101-1124, 1993; Unwin, N. Acetycholine receptor channel imaged in the open state. Nature 373:37-43, 1995.
7. Unwin, N. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229:1101-1124, 1993; Unwin, N. Acetycholine receptor channel imaged in the open state. Nature 373:37-43, 1995.
8. + channels, see: Miller, C. 1990: Annus mirabilis of potassium channels. Science 252:1092-1096, 1991; Jan, L.Y., Jan, Y.N. Potassium channels and their evolving gates. Nature 371:119-122, 1994.
9. + channels, see: Miller, C. 1990: Annus mirabilis of potassium channels. Science 252:1092-1096, 1991; Jan, L.Y., Jan, Y.N. Potassium channels and their evolving gates. Nature 371:119-122, 1994.
10. + channel signature sequence. Biophys. J. 66:1061-1067, 1994.
11. + channel: Expression cloning and molecular properties. Proc. Natl. Acad. Sci. U.S.A. 90:10235-10239, 1993; Kubo, Y., Reuveny, E., Slesinger, P.A., Jan, Y.N., Jan, L.Y. Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel. Nature 364:802-806, 1993; Lester, H.A., Dascal, N. The response to vagusstoff. Nature 364: 758-759, 1993.
12. + channel: Expression cloning and molecular properties. Proc. Natl. Acad. Sci. U.S.A. 90:10235-10239, 1993; Kubo, Y., Reuveny, E., Slesinger, P.A., Jan, Y.N., Jan, L.Y. Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel. Nature 364:802-806, 1993; Lester, H.A., Dascal, N. The response to vagusstoff. Nature 364: 758-759, 1993.
13. + channel: Expression cloning and molecular properties. Proc. Natl. Acad. Sci. U.S.A. 90:10235-10239, 1993; Kubo, Y., Reuveny, E., Slesinger, P.A., Jan, Y.N., Jan, L.Y. Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel. Nature 364:802-806, 1993; Lester, H.A., Dascal, N. The response to vagusstoff. Nature 364: 758-759, 1993.
14. For a recent discussion, see Mislow, K. A commentary on the topological chirality and achirality of molecules. Croat. Chem. Acta 69:485-511, 1996.
15. + channel. J. Biol. Chem. 271:30524-30528, 1996.
16. + channel: Subunit stoichiometry and structural domains essential for G protein stimulation. Am. Physiol. Soc. H379-H385, 1996. See also: Yang, J., Y.N. Jan, L.Y. Jan. Determination of the subunit stoichiometry of an inwardly rectifying potassium channel. Neuron 15:1441-1447, 1995; Isacoff, E.Y., Y.N. Jan, L.Y. Jan. Evidence for the formation of heteromultimeric potassium channels in xenopus-oocytes. Nature 345:530-534, 1990; Kavanaugh, M.P., Hurst, R.S., Yakel, J., Varnum, M.D., Adelman, J.P., North, R.A. Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium. Neuron 8:493-497, 1992.
17. + channel: Subunit stoichiometry and structural domains essential for G protein stimulation. Am. Physiol. Soc. H379-H385, 1996. See also: Yang, J., Y.N. Jan, L.Y. Jan. Determination of the subunit stoichiometry of an inwardly rectifying potassium channel. Neuron 15:1441-1447, 1995; Isacoff, E.Y., Y.N. Jan, L.Y. Jan. Evidence for the formation of heteromultimeric potassium channels in xenopus-oocytes. Nature 345:530-534, 1990; Kavanaugh, M.P., Hurst, R.S., Yakel, J., Varnum, M.D., Adelman, J.P., North, R.A. Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium. Neuron 8:493-497, 1992.
18. + channel: Subunit stoichiometry and structural domains essential for G protein stimulation. Am. Physiol. Soc. H379-H385, 1996. See also: Yang, J., Y.N. Jan, L.Y. Jan. Determination of the subunit stoichiometry of an inwardly rectifying potassium channel. Neuron 15:1441-1447, 1995; Isacoff, E.Y., Y.N. Jan, L.Y. Jan. Evidence for the formation of heteromultimeric potassium channels in xenopus-oocytes. Nature 345:530-534, 1990; Kavanaugh, M.P., Hurst, R.S., Yakel, J., Varnum, M.D., Adelman, J.P., North, R.A. Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium. Neuron 8:493-497, 1992.
19. + channel: Subunit stoichiometry and structural domains essential for G protein stimulation. Am. Physiol. Soc. H379-H385, 1996. See also: Yang, J., Y.N. Jan, L.Y. Jan. Determination of the subunit stoichiometry of an inwardly rectifying potassium channel. Neuron 15:1441-1447, 1995; Isacoff, E.Y., Y.N. Jan, L.Y. Jan. Evidence for the formation of heteromultimeric potassium channels in xenopus-oocytes. Nature 345:530-534, 1990; Kavanaugh, M.P., Hurst, R.S., Yakel, J., Varnum, M.D., Adelman, J.P., North, R.A. Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium. Neuron 8:493-497, 1992.
20. Charnet, P., Labarca, C., Leonard, R.J., Vogelaar, N.J., Czyzyk, L., Gouin, A., Davidson, N., Lester, H.A. An open-channel blocker interacts with adjacent turns of α-helices in the nicotinic acetycholine receptor. Neuron 2:87-95, 1990; Revah, F., Bertrand, D., Galzi, J.-L., Devillers-Thiéry, A., Mulle, C., Hussy, N., Bertrand, S., Ballivet, M., Changeux, J.-P. Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor. Nature 353:846-849, 1991.
21. Charnet, P., Labarca, C., Leonard, R.J., Vogelaar, N.J., Czyzyk, L., Gouin, A., Davidson, N., Lester, H.A. An open-channel blocker interacts with adjacent turns of α-helices in the nicotinic acetycholine receptor. Neuron 2:87-95, 1990; Revah, F., Bertrand, D., Galzi, J.-L., Devillers-Thiéry, A., Mulle, C., Hussy, N., Bertrand, S., Ballivet, M., Changeux, J.-P. Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor. Nature 353:846-849, 1991.
22. Labarca, C., Nowak, M.W., Zhang, H., Tang, L., Deshpande, P., Lester, H.A. Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors. Nature 376:514-516, 1995.
23. Kearney, P.C., Zhang, H., Zhong, W., Dougherty, D.A., Lester, H.A. 95. Determinants of nicotinic receptor gating in natural and unnatural side chain structures at the M2 9′ position. Neuron 17:1221-1229, 1996.
24. Filatov, G.N., White, M.M. The role of conserved leucines in the M2 domain of the acetylcholine-receptor in channel gating. Mol. Pharm. 48:379-384, 1995.
25. Gln for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression. J. Biol. Chem. 271:23169-23175, 1996; Kearney, P.C., Nowak, N.W., Zhong, W., Silverman, S., K., Lester, H.A., Dougherty, D.A. Dose-response relations for unnatural amino acids at the agonist binding site of the nicotinic acetylcholine receptor: Tests with novel side chains and with several agonists. Mol. Pharm. 50:1401-1412, 1996.
26. Gln for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression. J. Biol. Chem. 271:23169-23175, 1996; Kearney, P.C., Nowak, N.W., Zhong, W., Silverman, S., K., Lester, H.A., Dougherty, D.A. Dose-response relations for unnatural amino acids at the agonist binding site of the nicotinic acetylcholine receptor: Tests with novel side chains and with several agonists. Mol. Pharm. 50:1401-1412, 1996.
27. Gln for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression. J. Biol. Chem. 271:23169-23175, 1996; Kearney, P.C., Nowak, N.W., Zhong, W., Silverman, S., K., Lester, H.A., Dougherty, D.A. Dose-response relations for unnatural amino acids at the agonist binding site of the nicotinic acetylcholine receptor: Tests with novel side chains and with several agonists. Mol. Pharm. 50:1401-1412, 1996.
28. Machold, J., Weise, C., Utkin, Y., Tsetlin, V., Hucho, F. The handedness of the subunit arrangement of the nicotinic acetylcholine receptor from Torpedo californica. Eur. J. Biochem. 234:427-430, 1995.
29. Iwamura, H., Mislow, K. Stereochemical consequences of dynamic gearing. Acc. Chem. Res. 21:175-182, 1988.
30. Chance, J.M., Geiger, J.H., Okamoto, Y., Aburatani, R., Mislow, K. Stereochemical consequences of a parity restriction on dynamic gearing in tris(9-triptycyl)germanium chloride and tris(9-triptycyl)-cyclopropenium perchlorate. J. Am. Chem. Soc. 112:3540-3547, 1990.