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Volumn 263, Issue 2, 1996, Pages 297-310

A consensus structure for ω-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: Comparison of MVIIA, SVIB and SNX-202

Author keywords

Nuclear magnetic resonance; Peptide solution structure; Voltage sensitive calcium channel antagonist; conotoxin

Indexed keywords

CALCIUM CHANNEL; CALCIUM CHANNEL BLOCKING AGENT; OMEGA CONOTOXIN; OMEGA CONOTOXIN MVIIA; PEPTIDE;

EID: 0030601856     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0576     Document Type: Article
Times cited : (87)

References (53)
  • 1
    • 0025055598 scopus 로고
    • ω-Agatoxins: Novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom
    • Adams, M. E., Bindokas, V. P., Hasegawa, L. & Venema, V. J. (1990). ω-Agatoxins: novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom. J. Biol. Chem. 265, 861-878.
    • (1990) J. Biol. Chem. , vol.265 , pp. 861-878
    • Adams, M.E.1    Bindokas, V.P.2    Hasegawa, L.3    Venema, V.J.4
  • 2
    • 0028984720 scopus 로고
    • Solution structure of ω-conotoxin MVIIA using 2D NMR spectroscopy
    • Basus, V. J., Nadasdi, L., Ramachandran, J. & Miljanich, G. P. (1995). Solution structure of ω-conotoxin MVIIA using 2D NMR spectroscopy. FEBS Letters, 370, 163-169.
    • (1995) FEBS Letters , vol.370 , pp. 163-169
    • Basus, V.J.1    Nadasdi, L.2    Ramachandran, J.3    Miljanich, G.P.4
  • 3
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D. G. (1985). MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 4
    • 0024358239 scopus 로고
    • ω-Aga-I: A presynaptic calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta
    • Bindokas, V. P. & Adams, M. E. (1989). ω-Aga-I: a presynaptic calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta. J. Neurobiol. 20, 171-188.
    • (1989) J. Neurobiol. , vol.20 , pp. 171-188
    • Bindokas, V.P.1    Adams, M.E.2
  • 5
    • 0025916913 scopus 로고
    • Differential antagonism of transmitter release by subtypes of ω-agatoxins
    • Bindokas, V. P., Venema, V. J. & Adams, M. E. (1991). Differential antagonism of transmitter release by subtypes of ω-agatoxins. J. Neurophysiol. 66, 590-601.
    • (1991) J. Neurophysiol. , vol.66 , pp. 590-601
    • Bindokas, V.P.1    Venema, V.J.2    Adams, M.E.3
  • 9
    • 0000870109 scopus 로고
    • Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: Application to crambin
    • Brunger, A. T., Clore, G. M., Gronenborn, A. M. & Karplus, M. (1986). Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin. Proc. Natl Acad. Sci. USA 83, 3801-3805.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 3801-3805
    • Brunger, A.T.1    Clore, G.M.2    Gronenborn, A.M.3    Karplus, M.4
  • 10
    • 0027205407 scopus 로고
    • Solution structure of ω-conotoxin GVIA using 2-D NMR spectroscopy and relaxation matrix analysis
    • Davis, J. H., Bradley, E. K., Miljanich, G. P., Nadasdi, L., Ramachandran, J. & Basus, V. J. (1993). Solution structure of ω-conotoxin GVIA using 2-D NMR spectroscopy and relaxation matrix analysis. Biochemistry, 32, 7396-7405.
    • (1993) Biochemistry , vol.32 , pp. 7396-7405
    • Davis, J.H.1    Bradley, E.K.2    Miljanich, G.P.3    Nadasdi, L.4    Ramachandran, J.5    Basus, V.J.6
  • 11
    • 0028096838 scopus 로고
    • Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin
    • Ellinor, P. T., Zhang, J-F., Horne, W. A. & Tsien, R. W. (1994). Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin. Nature, 372, 272-275.
    • (1994) Nature , vol.372 , pp. 272-275
    • Ellinor, P.T.1    Zhang, J.-F.2    Horne, W.A.3    Tsien, R.W.4
  • 13
    • 0345311136 scopus 로고
    • Practical aspects of the E. COSY technique. Measurements of scalar spin-spin coupling constants in peptides
    • Greisinger, C., Sorenson, O. W. & Ernst, R. R. (1987). Practical aspects of the E. COSY technique. Measurements of scalar spin-spin coupling constants in peptides. J. Magn. Reson. 75, 474-492.
    • (1987) J. Magn. Reson. , vol.75 , pp. 474-492
    • Greisinger, C.1    Sorenson, O.W.2    Ernst, R.R.3
  • 14
    • 0027426430 scopus 로고
    • Biotinylated derivatives of ω-conotoxins GVIA and MVIID: Probes for neuronal calcium channels
    • Haack, J., Kinser, P., Yoshikami, D. & Olivera, B. (1993). Biotinylated derivatives of ω-conotoxins GVIA and MVIID: probes for neuronal calcium channels. Neuropharmacology, 32, 1151-1159.
    • (1993) Neuropharmacology , vol.32 , pp. 1151-1159
    • Haack, J.1    Kinser, P.2    Yoshikami, D.3    Olivera, B.4
  • 16
    • 0027092679 scopus 로고
    • The solution structure of eglin C based on the measurement of many NOEs and coupling constants and its comparison with X-ray structures
    • Hyberts, S. G., Goldberg, M. S., Havel, T. S. & Wagner, G. (1992). The solution structure of eglin C based on the measurement of many NOEs and coupling constants and its comparison with X-ray structures. Protein Sci. 1, 736-751.
    • (1992) Protein Sci. , vol.1 , pp. 736-751
    • Hyberts, S.G.1    Goldberg, M.S.2    Havel, T.S.3    Wagner, G.4
  • 17
    • 0343359244 scopus 로고
    • Investigation of chemical exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P. & Ernst, R. R. (1979). Investigation of chemical exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 20
    • 0029127283 scopus 로고
    • Three-dimensional structure in solution of the calcium channel blocker ω-conotoxin MVIIA
    • Kohno, T., Kim, J. I., Kobayashi, K., Kodera, Y., Maeda, T. & Sato, K. (1995). Three-dimensional structure in solution of the calcium channel blocker ω-conotoxin MVIIA. Biochemistry, 34, 10256-10265.
    • (1995) Biochemistry , vol.34 , pp. 10256-10265
    • Kohno, T.1    Kim, J.I.2    Kobayashi, K.3    Kodera, Y.4    Maeda, T.5    Sato, K.6
  • 21
    • 0019327003 scopus 로고
    • A two-dimensional nuclear overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A., Ernst, R. R. & Wuthrich, K. (1980). A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 22
    • 0024791275 scopus 로고
    • Distance geometry
    • (Oppenheimer, N. J. & James, T. L., eds), Academic Press, Inc., San Diego
    • Kuntz, I. D., Thomason, J. F. & Oshiro, C. M. (1989). Distance Geometry. In Methods in Enzymology (Oppenheimer, N. J. & James, T. L., eds), vol. 177, pp. 159-204, Academic Press, Inc., San Diego.
    • (1989) Methods in Enzymology , vol.177 , pp. 159-204
    • Kuntz, I.D.1    Thomason, J.F.2    Oshiro, C.M.3
  • 24
    • 0027512113 scopus 로고
    • Characterization and 2D NMR study of the stable (9-21, 15-27) 2 disulphide intermediate in the folding of the 3 disulphide trypsin inhibitor EETI II
    • Le-Nguyen, D., Heitz, A., Chiche, L., El Hajji, M. & Castro, B. (1993). Characterization and 2D NMR study of the stable (9-21, 15-27) 2 disulphide intermediate in the folding of the 3 disulphide trypsin inhibitor EETI II. Protein Sci. 2, 165-174.
    • (1993) Protein Sci. , vol.2 , pp. 165-174
    • Le-Nguyen, D.1    Heitz, A.2    Chiche, L.3    El Hajji, M.4    Castro, B.5
  • 26
    • 0028987884 scopus 로고
    • Antagonists of neuronal calcium channels: Structure, function and therapeutic implications
    • Miljanich, G. P. & Ramachandran, J. (1995). Antagonists of neuronal calcium channels: structure, function and therapeutic implications. Annu. Rev. Pharmacol. Toxicol. 35, 707-734.
    • (1995) Annu. Rev. Pharmacol. Toxicol. , vol.35 , pp. 707-734
    • Miljanich, G.P.1    Ramachandran, J.2
  • 31
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Fund. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Fund. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 33
  • 34
    • 0028292145 scopus 로고
    • Calcium channel diversity and neurotransmitter release: The ω-conotoxins and ω-agatoxins
    • Olivera, B. M., Miljanich, G. P., Ramachandran, J. & Adams, M. E. (1994). Calcium channel diversity and neurotransmitter release: the ω-conotoxins and ω-agatoxins. Annu. Rev. Biochem. 63, 823-867.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 823-867
    • Olivera, B.M.1    Miljanich, G.P.2    Ramachandran, J.3    Adams, M.E.4
  • 35
    • 0027379001 scopus 로고
    • Three-dimensional structure in solution of the calcium channel blocker ω-conotoxin
    • Pallaghy, P. K., Duggan, B. M., Pennington, M. W. & Norton, R. S. (1993). Three-dimensional structure in solution of the calcium channel blocker ω-conotoxin. J. Mol. Biol. 234, 405-420.
    • (1993) J. Mol. Biol. , vol.234 , pp. 405-420
    • Pallaghy, P.K.1    Duggan, B.M.2    Pennington, M.W.3    Norton, R.S.4
  • 36
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cysteine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides
    • Pallaghy, P. K., Nielsen, K. J., Craik, D. J. & Norton, R. S. (1994). A common structural motif incorporating a cysteine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides. Protein Sci. 3, 1833-1839.
    • (1994) Protein Sci. , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 38
    • 0001202015 scopus 로고
    • The relationship between chemical shift and secondary structure in proteins
    • Pastore, A. & Saudek, V. (1990). The relationship between chemical shift and secondary structure in proteins. J. Magn. Reson. 90, 165-176.
    • (1990) J. Magn. Reson. , vol.90 , pp. 165-176
    • Pastore, A.1    Saudek, V.2
  • 39
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. & Sklenár, V. (1992). Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR, 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 40
    • 0020648054 scopus 로고
    • Theory of protein secondary structure and algorithm of its prediction
    • Ptitsyn, O. B. & Finkelstein, A. V. (1983). Theory of protein secondary structure and algorithm of its prediction. Biopolymers, 22, 15-25.
    • (1983) Biopolymers , vol.22 , pp. 15-25
    • Ptitsyn, O.B.1    Finkelstein, A.V.2
  • 45
    • 0027517346 scopus 로고
    • Solution structure of the calcium channel antagonist ω-conotxin GVIA
    • Skalicky, J. J., Metzler, W. J., Ciesla, D. J., Galdes, A. & Pardi, A. (1993). Solution structure of the calcium channel antagonist ω-conotxin GVIA. Protein Sci. 2, 1591-1603.
    • (1993) Protein Sci. , vol.2 , pp. 1591-1603
    • Skalicky, J.J.1    Metzler, W.J.2    Ciesla, D.J.3    Galdes, A.4    Pardi, A.5
  • 46
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sönnichsen, F. D., van Eyk, J. E., Hodges, R. S. & Sykes, B. D. (1992). Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry, 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 47
    • 0026802393 scopus 로고
    • Antagonism of synaptosomal calcium channels by subtypes of ω-agatoxins
    • Venema, V. J., Swiderek, K. M., Lee, T. D., Hathaway, G. M. & Adams, M. E. (1992). Antagonism of synaptosomal calcium channels by subtypes of ω-agatoxins. J. Biol. Chem. 267, 2610-2615.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2610-2615
    • Venema, V.J.1    Swiderek, K.M.2    Lee, T.D.3    Hathaway, G.M.4    Adams, M.E.5
  • 48
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined by two different algorithms, DISGEO and DISMAN
    • Wagner, G., Braun, W., Havel, T. F., Schaumann, T., Go, N. & Wüthrich, K. (1987). Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined by two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196, 611-639.
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wüthrich, K.6
  • 49
    • 0025113022 scopus 로고
    • β-turns and their distortions: A proposed new nomenclature
    • Wilmot, C. M. & Thornton, J. M. (1990). β-turns and their distortions: a proposed new nomenclature. Protein Eng. 3, 479-493.
    • (1990) Protein Eng. , vol.3 , pp. 479-493
    • Wilmot, C.M.1    Thornton, J.M.2
  • 50
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D. & Richards, F. M. (1991). Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 51
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR, 5, 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 53
    • 0021095743 scopus 로고
    • Pseudo structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • Wüthrich, K., Billeter, M. & Braun, W. (1983). Pseudo structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169, 949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3


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