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Volumn 5, Issue , 2015, Pages

Structural analysis of Clostridium botulinum neurotoxin type D as a platform for the development of targeted secretion inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN; BOTULINUM TOXIN TYPE D; HORMONE RECEPTOR; NEUROPEPTIDE RECEPTOR; RECOMBINANT PROTEIN; SOMATOTROPIN RELEASING HORMONE RECEPTOR;

EID: 84940885067     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep13397     Document Type: Article
Times cited : (13)

References (45)
  • 1
  • 2
    • 84868353871 scopus 로고    scopus 로고
    • Clinical uses of botulinum neurotoxins: Current indications, limitations and future developments
    • Chen, S. Clinical uses of botulinum neurotoxins: current indications, limitations and future developments. Toxins (Basel) 4, 913-939 (2012).
    • (2012) Toxins (Basel) , vol.4 , pp. 913-939
    • Chen, S.1
  • 3
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: A marvel of protein design
    • Montal, M. Botulinum neurotoxin: a marvel of protein design. Annu. Rev. Biochem. 79, 591-617 (2010).
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 591-617
    • Montal, M.1
  • 4
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with snare and sm proteins
    • Südhof, T. C. & Rothman, J. E. Membrane fusion: grappling with SNARE and SM proteins. Science 323, 474-477 (2009).
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 5
    • 35148834892 scopus 로고    scopus 로고
    • Cattle immune response to botulinum type d toxoid: Results of a vaccination study
    • Steinman, A., Galon, N., Arazi, A., Bar-Giora, Y. & Shpigel, N. Y. Cattle immune response to botulinum type D toxoid: results of a vaccination study. Vaccine 25, 7636-40 (2007).
    • (2007) Vaccine , vol.25 , pp. 7636-7640
    • Steinman, A.1    Galon, N.2    Arazi, A.3    Bar-Giora, Y.4    Shpigel, N.Y.5
  • 6
    • 0030897432 scopus 로고    scopus 로고
    • In vitro characterization of botulinum toxin types a, c and d action on human tissues: Combined electrophysiologic, pharmacologic and molecular biologic approaches
    • Coffield, J. A. et al. In vitro characterization of botulinum toxin types A, C and D action on human tissues: combined electrophysiologic, pharmacologic and molecular biologic approaches. J. Pharmacol. Exp. Ther. 280, 1489-1498 (1997).
    • (1997) J. Pharmacol. Exp. Ther , vol.280 , pp. 1489-1498
    • Coffield, J.A.1
  • 7
    • 84876107497 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype d is poorly effective in humans: An in vivo electrophysiological study
    • Eleopra, R. et al. Botulinum neurotoxin serotype D is poorly effective in humans: an in vivo electrophysiological study. Clin. Neurophysiol. 124, 999-1004 (2013).
    • (2013) Clin. Neurophysiol , vol.124 , pp. 999-1004
    • Eleopra, R.1
  • 8
    • 79960680902 scopus 로고    scopus 로고
    • Novel ganglioside-mediated entry of botulinum neurotoxin serotype d into neurons
    • Kroken, A. R., Karalewitz, A. P.-A., Fu, Z., Kim, J.-J. P. & Barbieri, J. T. Novel ganglioside-mediated entry of botulinum neurotoxin serotype D into neurons. J. Biol. Chem. 286, 26828-26837 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 26828-26837
    • Kroken, A.R.1    Karalewitz, A.P.-A.2    Fu, Z.3    Kim, J.-J.P.4    Barbieri, J.T.5
  • 9
    • 79953289881 scopus 로고    scopus 로고
    • Botulinum neurotoxin d uses synaptic vesicle protein sv2 and gangliosides as receptors
    • Peng, L., Tepp, W. H., Johnson, E. A. & Dong, M. Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors. PLoS Pathog. 7, e1002008 (2011).
    • (2011) PLoS Pathog , vol.7 , pp. e1002008
    • Peng, L.1    Tepp, W.H.2    Johnson, E.A.3    Dong, M.4
  • 10
    • 0027366557 scopus 로고
    • Identification of the nerve terminal targets of botulinum neurotoxin serotypes a d, and e
    • Schiavo, G. et al. Identification of the nerve terminal targets of botulinum neurotoxin serotypes A, D, and E. J. Biol. Chem. 268, 23784-23787 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 23784-23787
    • Schiavo, G.1
  • 13
    • 84865975652 scopus 로고    scopus 로고
    • A botulinum toxin-derived targeted secretion inhibitor downregulates the gh/igf1 axis
    • Somm, E. et al. A botulinum toxin-derived targeted secretion inhibitor downregulates the GH/IGF1 axis. J. Clin. Invest. 122, 3295-3306 (2012).
    • (2012) J. Clin. Invest , vol.122 , pp. 3295-3306
    • Somm, E.1
  • 14
    • 84883142608 scopus 로고    scopus 로고
    • Ghrh receptor-targeted botulinum neurotoxin selectively inhibits pulsatile gh secretion in male rats
    • Leggett, J. et al. GHRH receptor-targeted botulinum neurotoxin selectively inhibits pulsatile GH secretion in male rats. Endocrinology 154, 3305-3318 (2013).
    • (2013) Endocrinology , vol.154 , pp. 3305-3318
    • Leggett, J.1
  • 15
    • 84886534177 scopus 로고    scopus 로고
    • Comparative inhibition of the gh/igf-i axis obtained with either the targeted secretion inhibitor sxn101959 or the somatostatin analog octreotide in growing male rats
    • Somm, E. et al. Comparative inhibition of the GH/IGF-I axis obtained with either the targeted secretion inhibitor SXN101959 or the somatostatin analog octreotide in growing male rats. Endocrinology 154, 4237-4248 (2013).
    • (2013) Endocrinology , vol.154 , pp. 4237-4248
    • Somm, E.1
  • 16
    • 33747194443 scopus 로고    scopus 로고
    • Re-engineering the target specificity of clostridial neurotoxins-A route to novel therapeutics
    • Foster, K. A. et al. Re-engineering the target specificity of Clostridial neurotoxins-A route to novel therapeutics. Neurotox. Res. 9, 101-7 (2006).
    • (2006) Neurotox. Res , vol.9 , pp. 101-107
    • Foster, K.A.1
  • 17
    • 61649127494 scopus 로고    scopus 로고
    • Crystal structure of a catalytically active, non-toxic endopeptidase derivative of clostridium botulinum toxin a
    • Masuyer, G. et al. Crystal structure of a catalytically active, non-toxic endopeptidase derivative of Clostridium botulinum toxin A. Biochem. Biophys. Res. Commun. 381, 50-53 (2009).
    • (2009) Biochem. Biophys. Res. Commun , vol.381 , pp. 50-53
    • Masuyer, G.1
  • 18
    • 79952452708 scopus 로고    scopus 로고
    • Structure and activity of a functional derivative of clostridium botulinum neurotoxin b
    • Masuyer, G., Beard, M., Cadd, V. A., Chaddock, J. A. & Acharya, K. R. Structure and activity of a functional derivative of Clostridium botulinum neurotoxin B. J. Struct. Biol. 174, 52-57 (2011).
    • (2011) J. Struct. Biol , vol.174 , pp. 52-57
    • Masuyer, G.1    Beard, M.2    Cadd, V.A.3    Chaddock, J.A.4    Acharya, K.R.5
  • 19
    • 0031712779 scopus 로고    scopus 로고
    • Crystal structure of botulinum neurotoxin type a and implications for toxicity
    • Lacy, D. B., Tepp, W., Cohen, A. C., DasGupta, B. R. & Stevens, R. C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat. Struct. Biol. 5, 898-902 (1998).
    • (1998) Nat. Struct. Biol , vol.5 , pp. 898-902
    • Lacy, D.B.1    Tepp, W.2    Cohen, A.C.3    DasGupta, B.R.4    Stevens, R.C.5
  • 20
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of clostridium botulinum neurotoxin b
    • Swaminathan, S. & Eswaramoorthy, S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 7, 693-699 (2000).
    • (2000) Nat. Struct. Biol , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 21
    • 58549116147 scopus 로고    scopus 로고
    • Domain organization in clostridium botulinum neurotoxin type e is unique: Its implication in faster translocation
    • Kumaran, D. et al. Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation. J. Mol. Biol. 386, 233-245 (2009).
    • (2009) J. Mol. Biol , vol.386 , pp. 233-245
    • Kumaran, D.1
  • 22
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 33644859288 scopus 로고    scopus 로고
    • Structure of botulinum neurotoxin type d light chain at 1.65a resolution: Repercussions for vamp-2 substrate specificity
    • Arndt, J. W., Chai, Q., Christian, T. & Stevens, R. C. Structure of botulinum neurotoxin type D light chain at 1.65A resolution: repercussions for VAMP-2 substrate specificity. Biochemistry 45, 3255-3262 (2006).
    • (2006) Biochemistry , vol.45 , pp. 3255-3262
    • Arndt, J.W.1    Chai, Q.2    Christian, T.3    Stevens, R.C.4
  • 24
    • 84884739450 scopus 로고    scopus 로고
    • Unique substrate recognition mechanism of the botulinum neurotoxin d light chain
    • Guo, J. & Chen, S. Unique substrate recognition mechanism of the botulinum neurotoxin D light chain. J. Biol. Chem. 288, 27881-27887 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 27881-27887
    • Guo, J.1    Chen, S.2
  • 25
    • 67650283952 scopus 로고    scopus 로고
    • Mode of vamp substrate recognition and inhibition of clostridium botulinum neurotoxin f
    • Agarwal, R., Schmidt, J. J., Stafford, R. G. & Swaminathan, S. Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F. Nat. Struct. Mol. Biol. 16, 789-794 (2009).
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 789-794
    • Agarwal, R.1    Schmidt, J.J.2    Stafford, R.G.3    Swaminathan, S.4
  • 26
    • 11144341950 scopus 로고    scopus 로고
    • Substrate recognition strategy for botulinum neurotoxin serotype a
    • Breidenbach, M. A. & Brunger, A. T. Substrate recognition strategy for botulinum neurotoxin serotype A. Nature 432, 925-929 (2004).
    • (2004) Nature , vol.432 , pp. 925-929
    • Breidenbach, M.A.1    Brunger, A.T.2
  • 27
    • 34848840291 scopus 로고    scopus 로고
    • Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain
    • Brünger, A. T. et al. Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain. PLoS Pathog. 3, 1191-1194 (2007).
    • (2007) PLoS Pathog , vol.3 , pp. 1191-1194
    • Brünger, A.T.1
  • 28
    • 51049104533 scopus 로고    scopus 로고
    • Substrate recognition mechanism of vamp/synaptobrevin-cleaving clostridial neurotoxins
    • Sikorra, S., Henke, T., Galli, T. & Binz, T. Substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins. J. Biol. Chem. 283, 21145-21152 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 21145-21152
    • Sikorra, S.1    Henke, T.2    Galli, T.3    Binz, T.4
  • 29
    • 55549106809 scopus 로고    scopus 로고
    • Membrane interaction of botulinum neurotoxin a translocation (t) domain. The belt region is a regulatory loop for membrane interaction
    • Galloux, M. et al. Membrane Interaction of botulinum neurotoxin A translocation (T) domain. The belt region is a regulatory loop for membrane interaction. J. Biol. Chem. 283, 27668-27676 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 27668-27676
    • Galloux, M.1
  • 30
    • 77958507818 scopus 로고    scopus 로고
    • Growth hormone-releasing hormone: Extrapituitary effects in physiology and pathology
    • Barabutis, N. & Schally, A. V. Growth hormone-releasing hormone: extrapituitary effects in physiology and pathology. Cell Cycle 9, 4110-4116 (2010).
    • (2010) Cell Cycle , vol.9 , pp. 4110-4116
    • Barabutis, N.1    Schally, A.V.2
  • 31
    • 0029185933 scopus 로고
    • Crysol-A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C. & Koch, M. H. J. Crysol-A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Cryst. 28, 768-773 (1995).
    • (1995) J. Appl. Cryst , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 32
    • 84907821952 scopus 로고    scopus 로고
    • New methods for indexing multi-lattice diffraction data
    • Gildea, R. J. et al. New methods for indexing multi-lattice diffraction data. Acta Crystallogr. D70, 2652-2666 (2014).
    • (2014) Acta Crystallogr , vol.D70 , pp. 2652-2666
    • Gildea, R.J.1
  • 33
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans, P. Scaling and assessment of data quality. Acta Crystallogr. D62, 72-82 (2006).
    • (2006) Acta Crystallogr , vol.D62 , pp. 72-82
    • Evans, P.1
  • 34
    • 0028103275 scopus 로고
    • The ccp4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta. Crystallogr. D50, 760-3 (1994).
    • (1994) Acta. Crystallogr , vol.D50 , pp. 760-763
  • 35
    • 84879367781 scopus 로고    scopus 로고
    • How good are my data and what is the resolution?
    • Evans, P. & Murshudov, G. N. How good are my data and what is the resolution? Acta Crystallogr. D69, 1204-1214 (2013).
    • (2013) Acta Crystallogr , vol.D69 , pp. 1204-1214
    • Evans, P.1    Murshudov, G.N.2
  • 36
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 37
    • 37349110734 scopus 로고    scopus 로고
    • Fitting molecular fragments into electron density
    • Cowtan, K. Fitting molecular fragments into electron density. Acta Crystallogr. D64, 83-89 (2008).
    • (2008) Acta Crystallogr , vol.D64 , pp. 83-89
    • Cowtan, K.1
  • 38
    • 79953763877 scopus 로고    scopus 로고
    • Refmac5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. et al. Refmac5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D67, 355-67 (2011).
    • (2011) Acta Crystallogr , vol.D67 , pp. 355-367
    • Murshudov, G.N.1
  • 40
    • 74549178560 scopus 로고    scopus 로고
    • Molprobity: All-Atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-Atom structure validation for macromolecular crystallography. Acta Crystallogr. D66, 12-21 (2010).
    • (2010) Acta Crystallogr , vol.D66 , pp. 12-21
    • Chen, V.B.1
  • 41
    • 84861499618 scopus 로고    scopus 로고
    • Instrumental setup for high-throughput small-And wide-Angle solution scattering at the x33 beamline of embl hamburg
    • Blanchet, C. E. et al. Instrumental setup for high-throughput small-And wide-Angle solution scattering at the X33 beamline of EMBL Hamburg. J. Appl. Cryst. 45, 489-495 (2012).
    • (2012) J. Appl. Cryst , vol.45 , pp. 489-495
    • Blanchet, C.E.1
  • 42
    • 0141484613 scopus 로고    scopus 로고
    • Primus: A windows pc-based system for smallangle scattering data analysis
    • Konarev, P. V., Volkov, V. V., Sokolova, A. V., Koch, M. H. J. & Svergun, D. I. PRIMUS: a Windows PC-based system for smallangle scattering data analysis. J. Appl. Cryst. 36, 1277-1282 (2003).
    • (2003) J. Appl. Cryst , Issue.36 , pp. 1277-1282
    • Konarev, P.V.1    Volkov, V.V.2    Sokolova, A.V.3    Koch, J.M.H.4    Svergun, D.I.5
  • 43
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 25, 495-503 (1992).
    • (1992) J. Appl. Cryst , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 44
    • 62649139615 scopus 로고    scopus 로고
    • Dammif a program for rapid ab-initio shape determination in small-Angle scattering
    • Franke, D. & Svergun, D. I. Dammif, a program for rapid ab-initio shape determination in small-Angle scattering. J. Appl. Cryst. 42, 342-346 (2009).
    • (2009) J. Appl. Cryst , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 45
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-Angle scattering
    • Volkov, V. V. & Svergun, D. I. Uniqueness of ab initio shape determination in small-Angle scattering. J. Appl. Cryst. 36, 860-864 (2003).
    • (2003) J. Appl. Cryst , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2


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