메뉴 건너뛰기




Volumn 7, Issue 2, 2000, Pages 143-151

Sexual attraction in the silkworm moth: Structure of the pheromone-binding-protein-bombykol complex

Author keywords

Chemical communication; Insect pheromone; Molecular recognition; Odorant binding protein; X ray crystallography

Indexed keywords

ANIMALIA; BOMBYCIDAE; BOMBYX MORI; HEXAPODA; INSECTA; LEPIDOPTERA;

EID: 0034141728     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)00078-8     Document Type: Article
Times cited : (426)

References (39)
  • 1
    • 0033595703 scopus 로고    scopus 로고
    • Olfactory reception in invertebrates
    • Krieger J., Breer H. Olfactory reception in invertebrates. Science. 286:1999;720-723.
    • (1999) Science , vol.286 , pp. 720-723
    • Krieger, J.1    Breer, H.2
  • 3
    • 0028789926 scopus 로고
    • Olfaction in lepidoptera
    • Hansson B.S. Olfaction in lepidoptera. Experientia. 51:1995;1003-1027.
    • (1995) Experientia , vol.51 , pp. 1003-1027
    • Hansson, B.S.1
  • 4
    • 0026695517 scopus 로고
    • 100 years of pheromone research: An essay on lepidoptera
    • Schneider D. 100 years of pheromone research: an essay on lepidoptera. Naturwissenschaften. 79:1992;241-250.
    • (1992) Naturwissenschaften , vol.79 , pp. 241-250
    • Schneider, D.1
  • 5
    • 0001681084 scopus 로고
    • Über den sexual-lockstoff des seidenspinners Bombyx mori. Reindarstellung and konstitution [On the sex attractant of the silkworm moth Bombyx mori. Isolation and structure]
    • Butenandt A, Beckmann R., Stamm D., Hecker E. Über den sexual-lockstoff des seidenspinners Bombyx mori. Reindarstellung and konstitution [On the sex attractant of the silkworm moth Bombyx mori. Isolation and structure]. Z. Natuforsch. B. 14:1959;283-284.
    • (1959) Z. Natuforsch. B , vol.14 , pp. 283-284
    • Butenandt, A.1    Beckmann, R.2    Stamm, D.3    Hecker, E.4
  • 6
    • 0001891786 scopus 로고
    • Bombykol revisited - reflections on a pioneering period and on some of its consequences
    • H.E. Hummel, & T.A. Miller. New York: Springer Verlag
    • Hecker E., Butenandt A. Bombykol revisited - reflections on a pioneering period and on some of its consequences. Hummel H.E., Miller T.A. Techniques in Pheromone Research. 1984;1-44 Springer Verlag, New York.
    • (1984) Techniques in Pheromone Research , pp. 1-44
    • Hecker, E.1    Butenandt, A.2
  • 7
    • 0014705889 scopus 로고
    • Die riechschwelle des seidenspinners [The olfactory threshold of the silkworm moth]
    • Kaissling K.-E., Priesner E Die riechschwelle des seidenspinners [The olfactory threshold of the silkworm moth]. Naturwissenschaften. 57:1970;23-28.
    • (1970) Naturwissenschaften , vol.57 , pp. 23-28
    • Kaissling, K.-E.1    Priesner, E.2
  • 8
    • 0019489601 scopus 로고
    • Pheromone binding and inactivation by moth antennae
    • Vogt R.G., Riddiford L.M. Pheromone binding and inactivation by moth antennae. Nature. 293:1981;161-163.
    • (1981) Nature , vol.293 , pp. 161-163
    • Vogt, R.G.1    Riddiford, L.M.2
  • 10
    • 0028894906 scopus 로고
    • Immunolocalisation of pheromone-binding protein and general odorant-binding protein in olfactory sensilla of the silk moths Antheraea and Bombyx
    • Steinbrecht R.A., Laue M., Ziegelberger G. Immunolocalisation of pheromone-binding protein and general odorant-binding protein in olfactory sensilla of the silk moths Antheraea and Bombyx. Cell Tissue Res. 282:1995;203-217.
    • (1995) Cell Tissue Res. , vol.282 , pp. 203-217
    • Steinbrecht, R.A.1    Laue, M.2    Ziegelberger, G.3
  • 12
    • 0000337895 scopus 로고
    • The pheromone binding protein of Bombyx mori: Purification, characterization, and immunocytochemical localization
    • Maida R., Steinbrecht A., Ziegelberger G., Pelosi P. The pheromone binding protein of Bombyx mori: purification, characterization, and immunocytochemical localization. Insect Biochem. Mol. Biol. 23:1993;243-253.
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 243-253
    • Maida, R.1    Steinbrecht, A.2    Ziegelberger, G.3    Pelosi, P.4
  • 13
    • 0029067645 scopus 로고
    • Protein structure encodes the ligand binding specificity in pheromone binding proteins
    • Du G., Prestwich G.D. Protein structure encodes the ligand binding specificity in pheromone binding proteins. Biochemistry. 34:1995;8726-8732.
    • (1995) Biochemistry , vol.34 , pp. 8726-8732
    • Du, G.1    Prestwich, G.D.2
  • 14
    • 0032725049 scopus 로고    scopus 로고
    • Conformational change in the pheromone binding protein from Bombyx mori induced by pH and by interaction with membranes
    • Wojtasek H., Leal W.S. Conformational change in the pheromone binding protein from Bombyx mori induced by pH and by interaction with membranes. J. Biol. Chem. 274:1999;30950-30956.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30950-30956
    • Wojtasek, H.1    Leal, W.S.2
  • 15
    • 0033432884 scopus 로고    scopus 로고
    • Disulfide structure of the pheromone binding protein from the silkworm moth, Bombyx mori
    • Leal W.S., Nikonova L., Peng G. Disulfide structure of the pheromone binding protein from the silkworm moth, Bombyx mori. FEBS Lett. 464:1999;85-90.
    • (1999) FEBS Lett. , vol.464 , pp. 85-90
    • Leal, W.S.1    Nikonova, L.2    Peng, G.3
  • 16
    • 0032474475 scopus 로고    scopus 로고
    • The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism
    • Spinelli S., Ramoni R., Grolli S., Bonicel J., Cambillau C., Tegoni M. The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Biochemistry. 37:1998;7913-7918.
    • (1998) Biochemistry , vol.37 , pp. 7913-7918
    • Spinelli, S.1    Ramoni, R.2    Grolli, S.3    Bonicel, J.4    Cambillau, C.5    Tegoni, M.6
  • 18
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: A molecular modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 19
    • 0033571068 scopus 로고    scopus 로고
    • A new class of hexahelical insect proteins revealed as putative carriers of small hydrophobic ligands
    • Rothenmund S., Liou Y.-C., Davies P.L., Krause E., Sönnichsen F.D. A new class of hexahelical insect proteins revealed as putative carriers of small hydrophobic ligands. Structure. 7:1999;1325-1332.
    • (1999) Structure , vol.7 , pp. 1325-1332
    • Rothenmund, S.1    Liou, Y.-C.2    Davies, P.L.3    Krause, E.4    Sönnichsen, F.D.5
  • 20
    • 0028583118 scopus 로고
    • Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing
    • Johnson B.H., Hecht M.H. Recombinant proteins can be isolated from E. coli cells by repeated cycles of freezing and thawing. Biotechnology. 12:1994;1357-1360.
    • (1994) Biotechnology , vol.12 , pp. 1357-1360
    • Johnson, B.H.1    Hecht, M.H.2
  • 21
    • 0031501013 scopus 로고    scopus 로고
    • A system for integrated collection and analysis of crystallographic diffraction data
    • Szebenyi D.M.E., Arvai A., Ealick S., LaIuppa J.M., Nielsen C. A system for integrated collection and analysis of crystallographic diffraction data. J. Synchrotron Rad. 4:1997;128-135.
    • (1997) J. Synchrotron Rad , vol.4 , pp. 128-135
    • Szebenyi, D.M.E.1    Arvai, A.2    Ealick, S.3    Laiuppa, J.M.4    Nielsen, C.5
  • 22
    • 0342657543 scopus 로고    scopus 로고
    • DPS: A data processing system for oscillation method data from a 2X2 Mosaic CCD Detector
    • Rossmann M. Abstract 11.06.06
    • Nielsen, C., et al., & Rossmann, M. (1998). DPS: A data processing system for oscillation method data from a 2X2 Mosaic CCD Detector. ACA Meeting July 18-23, Abstract 11.06.06.
    • (1998) ACA Meeting July 18-23
    • Nielsen, C.1
  • 23
    • 0000614826 scopus 로고    scopus 로고
    • An algorithm for automatic indexing of oscillation images using Fourier analysis
    • Steller I., Bolotovsky R., Rossmann M.G. An algorithm for automatic indexing of oscillation images using Fourier analysis. J. Appl. Crystallogr. 30:1997;1036-1040.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1036-1040
    • Steller, I.1    Bolotovsky, R.2    Rossmann, M.G.3
  • 24
    • 0000861898 scopus 로고    scopus 로고
    • The use of partial reflections for scaling and averaging x-ray area-detector data
    • Bolotovsky R., Steller I., Rossmann M.G. The use of partial reflections for scaling and averaging x-ray area-detector data. J. Appl. Crystallogr. 31:1998;708-717.
    • (1998) J. Appl. Crystallogr. , vol.31 , pp. 708-717
    • Bolotovsky, R.1    Steller, I.2    Rossmann, M.G.3
  • 25
    • 0002414103 scopus 로고
    • Molecular data processing
    • D. Moras, A.D. Pojarny, & J.C. Thierry. Oxford: Oxford University Press
    • Leslie A.G.W. Molecular data processing. Moras D., Pojarny A.D., Thierry J.C. Crystallographic Computing 5. 1990;50-61 Oxford University Press, Oxford.
    • (1990) Crystallographic Computing 5 , pp. 50-61
    • Leslie, A.G.W.1
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 28
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • De la Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 30
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger A.T., Warren G.L.et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 34
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:1988;10881-10890.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 35
    • 0027412196 scopus 로고
    • Alscript: A tool to format multiple sequence alignments
    • Barton G.J. Alscript: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 36
    • 0026244229 scopus 로고
    • MolScript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis J.P. MolScript: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, J.P.1
  • 37
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graphics. 15:1997;132-134.
    • (1997) J. Mol. Graphics , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 38
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 39
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.