메뉴 건너뛰기




Volumn 31, Issue 2, 2007, Pages 72-81

Computer modeling of binding of diverse weak toxins to nicotinic acetylcholine receptors

Author keywords

Nicotinic acetylcholine receptor; Non conventional toxins; Snake three finger toxins; Toxin receptor complex; Weak toxins

Indexed keywords

BIOLOGICAL TARGETS; NICOTINIC ACETYLCHOLINE RECEPTOR; NON-CONVENTIONAL TOXINS; SNAKE VENOMS TOXINS; TOXIN-RECEPTOR COMPLEX;

EID: 34047128667     PISSN: 14769271     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.compbiolchem.2007.02.011     Document Type: Article
Times cited : (20)

References (48)
  • 1
    • 0032971155 scopus 로고    scopus 로고
    • Primary structure of gamma-bungarotoxin, a new postsynaptic neurotoxin from venom of Bungarus multicinctus
    • Aird S.D., Womble G.C., Yates III J.R., and Griffin P.R. Primary structure of gamma-bungarotoxin, a new postsynaptic neurotoxin from venom of Bungarus multicinctus. Toxicon 37 4 (1999) 609-625
    • (1999) Toxicon , vol.37 , Issue.4 , pp. 609-625
    • Aird, S.D.1    Womble, G.C.2    Yates III, J.R.3    Griffin, P.R.4
  • 2
    • 0033521033 scopus 로고    scopus 로고
    • Variability among the sites by which curaremimetic toxins bind to Torpedo acetylcholine receptor, as revealed by identification of the functional residues of a-cobratoxin
    • Antil S., Servent D., and Menez A. Variability among the sites by which curaremimetic toxins bind to Torpedo acetylcholine receptor, as revealed by identification of the functional residues of a-cobratoxin. J. Biol. Chem. 274 (1999) 34851-34858
    • (1999) J. Biol. Chem. , vol.274 , pp. 34851-34858
    • Antil, S.1    Servent, D.2    Menez, A.3
  • 3
    • 0034703102 scopus 로고    scopus 로고
    • Molecular determinants by which a long chain toxin from snake venom interacts with the neuronal a7-nicotinic acetylcholine receptor
    • Antil-Delbeke S., Gaillard C., Tamiya T., Corringer P.J., Changeux J.P., Servent D., and Menez A. Molecular determinants by which a long chain toxin from snake venom interacts with the neuronal a7-nicotinic acetylcholine receptor. J. Biol. Chem. 275 (2000) 29594-29601
    • (2000) J. Biol. Chem. , vol.275 , pp. 29594-29601
    • Antil-Delbeke, S.1    Gaillard, C.2    Tamiya, T.3    Corringer, P.J.4    Changeux, J.P.5    Servent, D.6    Menez, A.7
  • 4
    • 18444411922 scopus 로고    scopus 로고
    • Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors
    • Bourne Y., Talley T.T., Hansen S.B., Taylor P., and Marchot P. Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors. EMBO J. 24 8 (2005) 1512-1522
    • (2005) EMBO J. , vol.24 , Issue.8 , pp. 1512-1522
    • Bourne, Y.1    Talley, T.T.2    Hansen, S.B.3    Taylor, P.4    Marchot, P.5
  • 6
    • 34047168122 scopus 로고    scopus 로고
    • Burkert, U., Allinger, N.L., 1982. Molecular Mechanics. ACS Monograph 177. American Chemical Society, Washington, DC.
  • 8
    • 52649173771 scopus 로고    scopus 로고
    • Characterization and gene organization of Taiwan banded krait (Bungarus multicinctus) γ-bungarotoxin
    • Chang L.-S., Chung C., Wu B., and Yang C. Characterization and gene organization of Taiwan banded krait (Bungarus multicinctus) γ-bungarotoxin. J. Prot. Chem. 21 4 (2002) 223-229
    • (2002) J. Prot. Chem. , vol.21 , Issue.4 , pp. 223-229
    • Chang, L.-S.1    Chung, C.2    Wu, B.3    Yang, C.4
  • 9
    • 0242286030 scopus 로고    scopus 로고
    • Novel neurotoxins from Taiwan banded krait (Bungarus multicinctus) venom: purification, characterization and gene organization
    • Chang L.-S., Chung C., Liou J.-C., Chang C.-W., and Yang C.-C. Novel neurotoxins from Taiwan banded krait (Bungarus multicinctus) venom: purification, characterization and gene organization. Toxicon 42 (2003) 323-330
    • (2003) Toxicon , vol.42 , pp. 323-330
    • Chang, L.-S.1    Chung, C.2    Liou, J.-C.3    Chang, C.-W.4    Yang, C.-C.5
  • 12
    • 0002687075 scopus 로고
    • Structure-function relationships of postsynaptic neurotoxins from snake venoms
    • Harvey A.L. (Ed), Pergamon Press, New York
    • Endo T., and Tamiya N. Structure-function relationships of postsynaptic neurotoxins from snake venoms. In: Harvey A.L. (Ed). Snake Toxins (1991), Pergamon Press, New York 165-222
    • (1991) Snake Toxins , pp. 165-222
    • Endo, T.1    Tamiya, N.2
  • 14
    • 15544369378 scopus 로고    scopus 로고
    • From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins
    • Fry B.G. From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Res. 15 3 (2005) 403-420
    • (2005) Genome Res. , vol.15 , Issue.3 , pp. 403-420
    • Fry, B.G.1
  • 16
    • 14844300820 scopus 로고    scopus 로고
    • Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence
    • Gao F., Bren N., Burghardt T.P., Hansen S., Henchman R.H., Taylor P., McCammon J.A., and Sine S.M. Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence. J. Biol. Chem. 280 9 (2005) 8443-8451
    • (2005) J. Biol. Chem. , vol.280 , Issue.9 , pp. 8443-8451
    • Gao, F.1    Bren, N.2    Burghardt, T.P.3    Hansen, S.4    Henchman, R.H.5    Taylor, P.6    McCammon, J.A.7    Sine, S.M.8
  • 17
    • 41349087737 scopus 로고    scopus 로고
    • Harmonic oscillators in the Nose-Hoover environment
    • Golo V.L., Salnikov V.N., and Shaitan K.V. Harmonic oscillators in the Nose-Hoover environment. Phys. Rev. E 70 (2004) 046130
    • (2004) Phys. Rev. E , vol.70 , pp. 046130
    • Golo, V.L.1    Salnikov, V.N.2    Shaitan, K.V.3
  • 18
    • 0040027144 scopus 로고    scopus 로고
    • Dynamic attractor for the Berendsen thermostat and the slow dynamics of biomacromolecules
    • Golo V.L., and Shaitan K.V. Dynamic attractor for the Berendsen thermostat and the slow dynamics of biomacromolecules. Biofizika 47 (2002) 611-617
    • (2002) Biofizika , vol.47 , pp. 611-617
    • Golo, V.L.1    Shaitan, K.V.2
  • 20
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen S.B., Sulzenbacher G., Huxford T., Marchot P., Taylor P., and Bourne Y. Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J. 24 20 (2005) 3635-3646
    • (2005) EMBO J. , vol.24 , Issue.20 , pp. 3635-3646
    • Hansen, S.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 23
    • 0001765604 scopus 로고
    • Chemistry of protein toxins in snake venoms
    • Lee C.Y. (Ed), Springer, Berlin
    • Karlsson E. Chemistry of protein toxins in snake venoms. In: Lee C.Y. (Ed). Snake Venoms, Handbook of Experimental Pharmacology vol. 52 (1979), Springer, Berlin 159-212
    • (1979) Snake Venoms, Handbook of Experimental Pharmacology , vol.52 , pp. 159-212
    • Karlsson, E.1
  • 24
    • 20444468955 scopus 로고    scopus 로고
    • Antibodies against native Naja kaouthia weak toxin WTX interacts with weak toxins and several other 3-finger toxins, but not with their denatured forms
    • Kryukova E.V., Mordvintsev D.Yu., Utkin Yu.N., and Tsetlin V.I. Antibodies against native Naja kaouthia weak toxin WTX interacts with weak toxins and several other 3-finger toxins, but not with their denatured forms. Toxicon 46 1 (2005) 24-30
    • (2005) Toxicon , vol.46 , Issue.1 , pp. 24-30
    • Kryukova, E.V.1    Mordvintsev, D.Yu.2    Utkin, Yu.N.3    Tsetlin, V.I.4
  • 25
    • 0033732304 scopus 로고    scopus 로고
    • The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methods
    • Kuhn P., Deakon A.M., Comoso S., Rajaseger G., Kini R.M., Uson I, and Kolatkar P.R. The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methods. Acta Crystallogr. Sect. D 56 (2000) 1401-1407
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 1401-1407
    • Kuhn, P.1    Deakon, A.M.2    Comoso, S.3    Rajaseger, G.4    Kini, R.M.5    Uson I6    Kolatkar, P.R.7
  • 26
    • 84949365205 scopus 로고
    • A comparison between collisional dynamics and Brownian dynamics
    • Lemak A.S., and Balabaev N.K. A comparison between collisional dynamics and Brownian dynamics. Mol. Simul. 15 (1995) 223-231
    • (1995) Mol. Simul. , vol.15 , pp. 223-231
    • Lemak, A.S.1    Balabaev, N.K.2
  • 27
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., and van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Mod. 7 (2001) 306-317
    • (2001) J. Mol. Mod. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 28
    • 28044455671 scopus 로고    scopus 로고
    • A model for short α-neurotoxin bound to nicotinic acetylcholine receptor from Torpedo californica: comparison with long-chain α-neurotoxins and α-conotoxins
    • Mordvintsev D.Y., Polyak Y.L., Levtsova O.V., Tourleigh Y.V., Kasheverov I.E., Shaitan K.V., Utkin Y.N., and Tsetlin V.I. A model for short α-neurotoxin bound to nicotinic acetylcholine receptor from Torpedo californica: comparison with long-chain α-neurotoxins and α-conotoxins. Comput. Biol. Chem. 29 6 (2005) 398-411
    • (2005) Comput. Biol. Chem. , vol.29 , Issue.6 , pp. 398-411
    • Mordvintsev, D.Y.1    Polyak, Y.L.2    Levtsova, O.V.3    Tourleigh, Y.V.4    Kasheverov, I.E.5    Shaitan, K.V.6    Utkin, Y.N.7    Tsetlin, V.I.8
  • 32
    • 1042268143 scopus 로고    scopus 로고
    • Three-finger alpha-neurotoxins and the nicotinic acetylcholine receptor, forty years on
    • Nirthanan S., and Gwee M.C. Three-finger alpha-neurotoxins and the nicotinic acetylcholine receptor, forty years on. J. Pharmacol. Sci. 94 1 (2004) 1-17
    • (2004) J. Pharmacol. Sci. , vol.94 , Issue.1 , pp. 1-17
    • Nirthanan, S.1    Gwee, M.C.2
  • 33
    • 9744270015 scopus 로고    scopus 로고
    • Weak neurotoxin from Naja kaouthia cobra venom affects haemodynamic regulation by acting on acetylcholine receptors
    • Ogay A.Y., Rzhevsky D.I., Murashev A.N., Tsetlin V.I., and Utkin Y.N. Weak neurotoxin from Naja kaouthia cobra venom affects haemodynamic regulation by acting on acetylcholine receptors. Toxicon 45 1 (2005) 93-99
    • (2005) Toxicon , vol.45 , Issue.1 , pp. 93-99
    • Ogay, A.Y.1    Rzhevsky, D.I.2    Murashev, A.N.3    Tsetlin, V.I.4    Utkin, Y.N.5
  • 34
    • 0001248201 scopus 로고    scopus 로고
    • NMR studies of a neurotoxin (candoxin) from Bungarus candidus-presence of a predominantly beta-sheeted structure
    • Parvathy V.R., Chary K.V.R., Kini R.M., and Govil G. NMR studies of a neurotoxin (candoxin) from Bungarus candidus-presence of a predominantly beta-sheeted structure. Curr. Sci. 79 (2000) 219-221
    • (2000) Curr. Sci. , vol.79 , pp. 219-221
    • Parvathy, V.R.1    Chary, K.V.R.2    Kini, R.M.3    Govil, G.4
  • 35
    • 0036042543 scopus 로고    scopus 로고
    • A synthetic weak neurotoxin binds with low affinity to Torpedo and chicken α7 nicotinic acetylcholine receptor
    • Poh S.L., Mourier Gr., Thai R., Armugam A., Molgo J., Servent D., Jeyaseelan K., and Menez A. A synthetic weak neurotoxin binds with low affinity to Torpedo and chicken α7 nicotinic acetylcholine receptor. Eur. J. Biochem. 269 (2002) 4247-4256
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4247-4256
    • Poh, S.L.1    Mourier, Gr.2    Thai, R.3    Armugam, A.4    Molgo, J.5    Servent, D.6    Jeyaseelan, K.7    Menez, A.8
  • 36
    • 0242443693 scopus 로고    scopus 로고
    • Force fields for protein simulations
    • Ponder J.W., and Case D.A. Force fields for protein simulations. Adv. Prot. Chem. 66 (2003) 27-85
    • (2003) Adv. Prot. Chem. , vol.66 , pp. 27-85
    • Ponder, J.W.1    Case, D.A.2
  • 37
    • 0035957581 scopus 로고    scopus 로고
    • Snake toxins that bind specifically to individual subtypes of muscarinic receptors
    • Potter L.T. Snake toxins that bind specifically to individual subtypes of muscarinic receptors. Life Sci. 68 22/23 (2001) 2541-2547
    • (2001) Life Sci. , vol.68 , Issue.22-23 , pp. 2541-2547
    • Potter, L.T.1
  • 38
    • 0028932758 scopus 로고
    • Solution structure of a green mamba toxin that activates muscarinic acetylcholine receptors, as studied by nuclear magnetic resonance and molecular modeling
    • Segalas I., Roumestand C., Zinn-Justin S., Gilquin B., Menez R., Menez A., and Toma F. Solution structure of a green mamba toxin that activates muscarinic acetylcholine receptors, as studied by nuclear magnetic resonance and molecular modeling. Biochemistry 34 (1995) 1248-1260
    • (1995) Biochemistry , vol.34 , pp. 1248-1260
    • Segalas, I.1    Roumestand, C.2    Zinn-Justin, S.3    Gilquin, B.4    Menez, R.5    Menez, A.6    Toma, F.7
  • 39
    • 0001607746 scopus 로고    scopus 로고
    • Snake neurotoxins that interact with nicotinic acetylcholine receptors
    • Massaro E.J. (Ed), Humana, Totowa, NJ
    • Servent D., and Menez A. Snake neurotoxins that interact with nicotinic acetylcholine receptors. In: Massaro E.J. (Ed). Handbook of Neurotoxicology vol. 1 (2001), Humana, Totowa, NJ 385-425
    • (2001) Handbook of Neurotoxicology , vol.1 , pp. 385-425
    • Servent, D.1    Menez, A.2
  • 40
    • 0037067680 scopus 로고    scopus 로고
    • How do short neurotoxins bind to a muscular-type nicotinic acetylcholine receptor?
    • Teixeira-Clerc F., Menez A., and Kessler P. How do short neurotoxins bind to a muscular-type nicotinic acetylcholine receptor?. J. Biol. Chem. 277 (2002) 25741-25747
    • (2002) J. Biol. Chem. , vol.277 , pp. 25741-25747
    • Teixeira-Clerc, F.1    Menez, A.2    Kessler, P.3
  • 41
    • 0035893751 scopus 로고    scopus 로고
    • NMR structure of bucandin, a neurotoxin from the venom of the Malayan krait (Bungarus candidus)
    • Torres A.M., Kini R.M., Nirthanan S., and Kuchel P.W. NMR structure of bucandin, a neurotoxin from the venom of the Malayan krait (Bungarus candidus). Biochem. J. 360 (2001) 539-548
    • (2001) Biochem. J. , vol.360 , pp. 539-548
    • Torres, A.M.1    Kini, R.M.2    Nirthanan, S.3    Kuchel, P.W.4
  • 42
    • 0028934293 scopus 로고
    • Genetic engineering of snake toxins. The functional site of erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues
    • Tremeaux O., Lemaire C., Drevet P., Pinkasfeld S., Ducancel F., Boulain J.C., and Menez A. Genetic engineering of snake toxins. The functional site of erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues. J. Biol. Chem. 270 (1995) 9362-9369
    • (1995) J. Biol. Chem. , vol.270 , pp. 9362-9369
    • Tremeaux, O.1    Lemaire, C.2    Drevet, P.3    Pinkasfeld, S.4    Ducancel, F.5    Boulain, J.C.6    Menez, A.7
  • 43
    • 0033198876 scopus 로고    scopus 로고
    • Snake venom alpha-neurotoxins and other 'three-finger' proteins
    • Tsetlin V. Snake venom alpha-neurotoxins and other 'three-finger' proteins. Eur. J. Biochem. 264 2 (1999) 281-286
    • (1999) Eur. J. Biochem. , vol.264 , Issue.2 , pp. 281-286
    • Tsetlin, V.1
  • 44
    • 1642450641 scopus 로고    scopus 로고
    • Snake and snail toxins acting on nicotinic acetylcholine receptors: fundamental aspects and medical applications
    • Tsetlin V.I., and Hucho F. Snake and snail toxins acting on nicotinic acetylcholine receptors: fundamental aspects and medical applications. FEBS Lett. 557 1-3 (2004) 9-13
    • (2004) FEBS Lett. , vol.557 , Issue.1-3 , pp. 9-13
    • Tsetlin, V.I.1    Hucho, F.2
  • 45
    • 33644870155 scopus 로고    scopus 로고
    • Structural determinants of selective {α}-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP
    • Ulens C., Hogg R.C., Celie P.H., Bertrand D., Tsetlin V., Smit A.B., and Sixma T.K. Structural determinants of selective {α}-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP. Proc. Natl. Acad. Sci. U.S.A. 103 10 (2006) 3615-3620
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , Issue.10 , pp. 3615-3620
    • Ulens, C.1    Hogg, R.C.2    Celie, P.H.3    Bertrand, D.4    Tsetlin, V.5    Smit, A.B.6    Sixma, T.K.7
  • 46
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin N. Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346 4 (2005) 967-989
    • (2005) J. Mol. Biol. , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 48


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.