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Volumn 29, Issue 3, 1997, Pages 391-398

Prediction of the secondary structure of the nicotinic acetylcholine receptor nontransmembrane regions

Author keywords

Automatic predictions; IR spectroscopy; Neural networks; RAMAN spectroscopy

Indexed keywords

CHOLINERGIC RECEPTOR; ION CHANNEL; NICOTINIC RECEPTOR; RECEPTOR SUBUNIT;

EID: 0030780210     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199711)29:3'391::AID-PROT12'3.0.CO;2-I     Document Type: Article
Times cited : (13)

References (43)
  • 1
    • 84916319138 scopus 로고
    • The secondary structure of acetylcholine-receptor reconstituted in a single lipid component as determined by ramanspectroscopy
    • Yager, P., Chang, E.L., Williams, R.W., Dalziel, A.W. The secondary structure of acetylcholine-receptor reconstituted in a single lipid component as determined by ramanspectroscopy. Biophys. J. 45:26-28, 1984.
    • (1984) Biophys. J. , vol.45 , pp. 26-28
    • Yager, P.1    Chang, E.L.2    Williams, R.W.3    Dalziel, A.W.4
  • 2
    • 0028361585 scopus 로고
    • Secondary structure of the nicotinic acetylcholine-receptor - Implications for structural models of a ligand-gated ion-channel
    • Méthot, N., McCarthy, M.P., Baenziger, J.E. Secondary structure of the nicotinic acetylcholine-receptor - Implications for structural models of a ligand-gated ion-channel. Biochemistry 33:7709-7717, 1994.
    • (1994) Biochemistry , vol.33 , pp. 7709-7717
    • Méthot, N.1    McCarthy, M.P.2    Baenziger, J.E.3
  • 3
    • 0028796049 scopus 로고
    • Evolutionary history of the ligand-gated ion-channel superfamily of receptors
    • Ortells, M.O., Lunt, G.G. Evolutionary history of the ligand-gated ion-channel superfamily of receptors. Trends Neurosci. 18:121-127, 1995a.
    • (1995) Trends Neurosci. , vol.18 , pp. 121-127
    • Ortells, M.O.1    Lunt, G.G.2
  • 4
    • 0343631524 scopus 로고
    • Evolution and desensitization of LGIC receptors
    • Ortells, M.O., Lunt, G.G. Evolution and desensitization of LGIC receptors. Trends Neurosci. 18:298-299, 1995b.
    • (1995) Trends Neurosci. , vol.18 , pp. 298-299
    • Ortells, M.O.1    Lunt, G.G.2
  • 5
    • 0027182846 scopus 로고
    • Structure of nicotinic acetylcholine receptors
    • Karlin, A. Structure of nicotinic acetylcholine receptors. Curr. Opin. Neurol. 3:299-309, 1993.
    • (1993) Curr. Opin. Neurol. , vol.3 , pp. 299-309
    • Karlin, A.1
  • 7
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin, N. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229:1101-1124, 1993.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 8
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. Acetylcholine receptor channel imaged in the open state. Nature 373:37-43, 1995.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 9
    • 0027954627 scopus 로고
    • The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β structures
    • Görne-Tschelnokow, U., Strecker, A., Kaduk, C., Naumann, D., Hucho, F. The transmembrane domains of the nicotinic acetylcholine receptor contain α-helical and β structures. EMBO J. 13:338-341, 1994.
    • (1994) EMBO J. , vol.13 , pp. 338-341
    • Görne-Tschelnokow, U.1    Strecker, A.2    Kaduk, C.3    Naumann, D.4    Hucho, F.5
  • 10
    • 0028242326 scopus 로고
    • The transmembrane region of the nicotinic acetylcholine receptor: Is it an all-helix bundle. Recept
    • Ortells, M. O., Lunt, G. The transmembrane region of the nicotinic acetylcholine receptor: Is it an all-helix bundle. Recept. Channels 2:53-59, 1994.
    • (1994) Channels , vol.2 , pp. 53-59
    • Ortells, M.O.1    Lunt, G.2
  • 11
    • 0029936679 scopus 로고    scopus 로고
    • A mixed helix-beta sheet model of the transmembrane region of the nicotinic acetylcholine receptor
    • Ortells, M.O., Lunt, G. A mixed helix-beta sheet model of the transmembrane region of the nicotinic acetylcholine receptor. Protein Eng. 9:51-59, 1996.
    • (1996) Protein Eng. , vol.9 , pp. 51-59
    • Ortells, M.O.1    Lunt, G.2
  • 12
    • 0010214174 scopus 로고
    • Amphipatic analysis and possible formation of the ion channel in an acetylcholine receptor
    • Finer-Moore, J., Stroud, R.M. Amphipatic analysis and possible formation of the ion channel in an acetylcholine receptor. Proc. Natl. Acad. Sci. USA 81:155-159, 1984.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 155-159
    • Finer-Moore, J.1    Stroud, R.M.2
  • 13
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D.J., Robson, B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97-120, 1978.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 14
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins, C., Bleasby, A.J., Fuchs, R. CLUSTAL V: Improved software for multiple sequence alignment. CABIOS 8:189-191, 1992.
    • (1992) CABIOS , vol.8 , pp. 189-191
    • Higgins, C.1    Bleasby, A.J.2    Fuchs, R.3
  • 15
    • 0027772024 scopus 로고
    • CEDIT: A C interface and macro facility for protein sequence alignment editing in colour with Microsoft Word 5.0 for PCs
    • Ortells, M.O., Cockcroft, V.B., Lunt, G. CEDIT: A C interface and macro facility for protein sequence alignment editing in colour with Microsoft Word 5.0 for PCs. CABIOS 9:741-744, 1993.
    • (1993) CABIOS , vol.9 , pp. 741-744
    • Ortells, M.O.1    Cockcroft, V.B.2    Lunt, G.3
  • 16
    • 0023050277 scopus 로고
    • An algorithm for secondary structure determination in proteins based on sequence similarity
    • Levin, J.M., Robson, B., Garnier, J. An algorithm for secondary structure determination in proteins based on sequence similarity. FEBS Lett. 205:303-308, 1986.
    • (1986) FEBS Lett. , vol.205 , pp. 303-308
    • Levin, J.M.1    Robson, B.2    Garnier, J.3
  • 17
    • 0001040367 scopus 로고
    • An algorithm for protein secondary structure prediction based on class prediction
    • Deleage, G., Roux, B. An algorithm for protein secondary structure prediction based on class prediction. Protein Eng. 1:289-294, 1987.
    • (1987) Protein Eng. , vol.1 , pp. 289-294
    • Deleage, G.1    Roux, B.2
  • 18
    • 0023555768 scopus 로고
    • Further developments of protein secondary structure prediction using information-theory - New parameters and consideration of residue pairs
    • Gibrat, J.F., Garnier, J., Robson, B. Further developments of protein secondary structure prediction using information-theory - New parameters and consideration of residue pairs. J. Mol. Biol. 198:425-443, 1987.
    • (1987) J. Mol. Biol. , vol.198 , pp. 425-443
    • Gibrat, J.F.1    Garnier, J.2    Robson, B.3
  • 19
    • 0000268209 scopus 로고
    • Protein secondary structure prediction with a neural network
    • Holley, H., Karplus, M. Protein secondary structure prediction with a neural network. Proc. Natl. Acad. Sci. USA 86:152-156, 1989.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 152-156
    • Holley, H.1    Karplus, M.2
  • 20
    • 0028009149 scopus 로고
    • SOPM: A self-optimized method for protein secondary structure prediction
    • Geourjon, C., Deléage, G. SOPM: A self-optimized method for protein secondary structure prediction. Protein Eng. 7:157-164, 1994.
    • (1994) Protein Eng. , vol.7 , pp. 157-164
    • Geourjon, C.1    Deléage, G.2
  • 21
    • 0000586923 scopus 로고
    • Predicting de novo the folded structure of proteins
    • Benner, S.A. Predicting de novo the folded structure of proteins. Curr. Opin. Struct. Biol. 2:402-412, 1992.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 402-412
    • Benner, S.A.1
  • 23
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70-percent accuracy
    • Rost, B., Sander, C. Prediction of protein secondary structure at better than 70-percent accuracy. J. Mol. Biol. 232:584-599, 1993.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 24
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., Sander, C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins Struct. Funct. Genet. 19:55-72, 1994.
    • (1994) Proteins Struct. Funct. Genet. , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 25
    • 0028783819 scopus 로고
    • Progress of 1d protein-structure prediction at last
    • Rost, B., Sander, C. Progress of 1d protein-structure prediction at last. Proteins Struct. Funct. Genet. 23:295-300, 1995.
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 295-300
    • Rost, B.1    Sander, C.2
  • 26
    • 0027202225 scopus 로고
    • Ftir analysis of nicotinic acetylcholine-receptor secondary structure in reconstituted membranes
    • Butler, D.H., McNamee, M.G. Ftir analysis of nicotinic acetylcholine-receptor secondary structure in reconstituted membranes. Bioch. Biophys. Acta 1150:17-24, 1993.
    • (1993) Bioch. Biophys. Acta , vol.1150 , pp. 17-24
    • Butler, D.H.1    McNamee, M.G.2
  • 28
    • 0023193779 scopus 로고
    • Stabilization of acetylcholine-receptor secondary structure by cholesterol and negatively charged phospholipids in membranes
    • Fong, T.M., McNamee, M.G. Stabilization of acetylcholine-receptor secondary structure by cholesterol and negatively charged phospholipids in membranes. Biochemistry 26: 3871-3880, 1987.
    • (1987) Biochemistry , vol.26 , pp. 3871-3880
    • Fong, T.M.1    McNamee, M.G.2
  • 29
    • 0023834873 scopus 로고
    • Secondary structural-analyses of the nicotinic acetylcholine-receptor as a test of molecular-models
    • Mielke, D.L., Wallace, B.A. Secondary structural-analyses of the nicotinic acetylcholine-receptor as a test of molecular-models. J. Biol. Chem. 263:3177-3182, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3177-3182
    • Mielke, D.L.1    Wallace, B.A.2
  • 30
    • 0025333463 scopus 로고
    • Conformation of acetylcholine-receptor in the presence of agonists and antagonists
    • Wu, C.-S.C, Sun, X.H., Yan, J.T. Conformation of acetylcholine-receptor in the presence of agonists and antagonists. J. Protein Chem. 9:119-126, 1990.
    • (1990) J. Protein Chem. , vol.9 , pp. 119-126
    • Wu, C.-S.C.1    Sun, X.H.2    Yan, J.T.3
  • 31
    • 0025884565 scopus 로고
    • Functional architecture of the nicotinic acetylcholine receptor: From electric organ to brain
    • Galzi, J.-L., Revah, F., Bessis, A., Changeux, J.-P. Functional architecture of the nicotinic acetylcholine receptor: From electric organ to brain. Annu. Rev. Pharmacol. Toxicol. 31:37-72, 1991.
    • (1991) Annu. Rev. Pharmacol. Toxicol. , vol.31 , pp. 37-72
    • Galzi, J.-L.1    Revah, F.2    Bessis, A.3    Changeux, J.-P.4
  • 32
    • 0027165974 scopus 로고
    • Acetylcholine receptor assembly: Subunit folding and oligomerization occur sequentially
    • Green, W.N., Claudio, T. Acetylcholine receptor assembly: Subunit folding and oligomerization occur sequentially. Cell 74:57-69, 1993.
    • (1993) Cell , vol.74 , pp. 57-69
    • Green, W.N.1    Claudio, T.2
  • 33
    • 0028914380 scopus 로고
    • Intersubunit contacts governing assembly of the mammalian nicotinic acetylcholine-receptor
    • Kreienkamp, H.J., Maeda, R.K., Sine, S.M., Taylor, P. Intersubunit contacts governing assembly of the mammalian nicotinic acetylcholine-receptor. Neuron 14:635-644, 1995.
    • (1995) Neuron , vol.14 , pp. 635-644
    • Kreienkamp, H.J.1    Maeda, R.K.2    Sine, S.M.3    Taylor, P.4
  • 34
    • 0026709052 scopus 로고
    • Assembly of mutant subunits of the nicotinic acetylcholine receptor lacking the conserved disulphide loop structure
    • Sumikawa, K., Gehle, V.M. Assembly of mutant subunits of the nicotinic acetylcholine receptor lacking the conserved disulphide loop structure. J. Biol. Chem. 267:6286-6290, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6286-6290
    • Sumikawa, K.1    Gehle, V.M.2
  • 35
    • 0026516536 scopus 로고
    • Sequences on the N-terminus of ACh receptor subunits regulate their assembly. Mo
    • Sumikawa, K. Sequences on the N-terminus of ACh receptor subunits regulate their assembly. Mol. Brain Res. 13:349-353, 1992.
    • (1992) L. Brain Res. , vol.13 , pp. 349-353
    • Sumikawa, K.1
  • 36
    • 0026595697 scopus 로고
    • The N-terminal domains of acetylcholine receptor subunits contain recognition signals for the initial steps of receptor assembly
    • Verrall, S., Hall, Z.W. The N-terminal domains of acetylcholine receptor subunits contain recognition signals for the initial steps of receptor assembly. Cell 68:23-31, 1992.
    • (1992) Cell , vol.68 , pp. 23-31
    • Verrall, S.1    Hall, Z.W.2
  • 37
    • 0028075109 scopus 로고
    • A sequence in the main cytoplasmic loop of the a subunit is required for assembly of mouse muscle nicotinic acetylcholine-receptor
    • Yu, X.M., Hall, Z.W. A sequence in the main cytoplasmic loop of the a subunit is required for assembly of mouse muscle nicotinic acetylcholine-receptor. Neuron 13:247-255, 1994.
    • (1994) Neuron , vol.13 , pp. 247-255
    • Yu, X.M.1    Hall, Z.W.2
  • 38
    • 0026536645 scopus 로고
    • Antagonism of ligand-gated ion channel receptors: Two domains of the glycine receptor Ó subunit form the strychnine-binding site
    • Vandenberg, R.J., French, C.R., Barry, P.H., Shine, J., Schofield, P.R. Antagonism of ligand-gated ion channel receptors: Two domains of the glycine receptor Ó subunit form the strychnine-binding site. Proc. Natl. Acad. Sci. USA 89:1765-1769, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1765-1769
    • Vandenberg, R.J.1    French, C.R.2    Barry, P.H.3    Shine, J.4    Schofield, P.R.5
  • 39
    • 0028952302 scopus 로고
    • Nicotine dependence, midbrain dopamine systems and psychiatric-disorders
    • Nisell, M., Nomikos, G.G., Svensson, T.H. Nicotine dependence, midbrain dopamine systems and psychiatric-disorders. Pharmacol. Toxicol. 76:157-162, 1995.
    • (1995) Pharmacol. Toxicol. , vol.76 , pp. 157-162
    • Nisell, M.1    Nomikos, G.G.2    Svensson, T.H.3
  • 40
    • 0027945601 scopus 로고
    • Neural mechanisms underlying nicotine dependence
    • Balfour, D.J.K. Neural mechanisms underlying nicotine dependence. Addiction 89:1419-1423, 1994.
    • (1994) Addiction , vol.89 , pp. 1419-1423
    • Balfour, D.J.K.1
  • 41
    • 0028962784 scopus 로고
    • Genetic and environmental aspects of the role of nicotinic receptors in neurodegenerative disorders - Emphasis on Alzheimer'disease and Parkinson's disease
    • James, J.R., Nordberg, A. Genetic and environmental aspects of the role of nicotinic receptors in neurodegenerative disorders - Emphasis on Alzheimer'disease and Parkinson's disease. Behav. Genet. 25:149-159, 1995.
    • (1995) Behav. Genet. , vol.25 , pp. 149-159
    • James, J.R.1    Nordberg, A.2
  • 42
    • 0028934741 scopus 로고
    • Improved learning and memory in aged rats with chronic administration of the nicotinic receptor agonist gts-21
    • Arendash, G.W., Sengstock, G.J., Sanberg, P.R., Kem, W.R. Improved learning and memory in aged rats with chronic administration of the nicotinic receptor agonist gts-21. Brain Res. 674:252-259, 1995.
    • (1995) Brain Res. , vol.674 , pp. 252-259
    • Arendash, G.W.1    Sengstock, G.J.2    Sanberg, P.R.3    Kem, W.R.4
  • 43
    • 0030912140 scopus 로고    scopus 로고
    • Molecular modelling of the nicotinic acetylcholine receptor transmembrane region in the open state
    • Ortells, M.O., Barrantes, G.E, Wood, C., Lunt, G.G., Barrantes, F.J. Molecular modelling of the nicotinic acetylcholine receptor transmembrane region in the open state. Protein. Eng. 10:511-517, 1997.
    • (1997) Protein. Eng. , vol.10 , pp. 511-517
    • Ortells, M.O.1    Barrantes, G.E.2    Wood, C.3    Lunt, G.G.4    Barrantes, F.J.5


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