메뉴 건너뛰기




Volumn 110, Issue 46, 2013, Pages 18680-18685

Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein

Author keywords

Amide proton exchange; Conformational equilibrium; Insect odorant binding protein; NMR structure; Selective transport of pheromones

Indexed keywords

BOMBYKOL; PHEROMONE; PHEROMONE BINDING PROTEIN; SEX HORMONE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84887421611     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1317706110     Document Type: Article
Times cited : (59)

References (45)
  • 3
    • 0014705889 scopus 로고
    • Die Riechschwelle des Seidenspinners
    • Kaissling KE, Priesner E (1970) Die Riechschwelle des Seidenspinners. Naturwissenschaften 57(1):23-28.
    • (1970) Naturwissenschaften , vol.57 , Issue.1 , pp. 23-28
    • Kaissling, K.E.1    Priesner, E.2
  • 4
    • 0002199052 scopus 로고
    • Zur Morphometrie der Antenne des Seidenspinners, Bombyx mori L.: Zahl und Verteilung der Riechsensillen
    • Steinbrecht RA (1970) Zur Morphometrie der Antenne des Seidenspinners, Bombyx mori L.: Zahl und Verteilung der Riechsensillen. Zeitschrift für Morphologie der Tiere 68(2):93-126.
    • (1970) Zeitschrift für Morphologie der Tiere , vol.68 , Issue.2 , pp. 93-126
    • Steinbrecht, R.A.1
  • 6
    • 84873807676 scopus 로고    scopus 로고
    • Odorant reception in insects: Roles of receptors, binding proteins, and degrading enzymes
    • Leal WS (2013) Odorant reception in insects: Roles of receptors, binding proteins, and degrading enzymes. Annu Rev Entomol 58:373-391.
    • (2013) Annu Rev Entomol , vol.58 , pp. 373-391
    • Leal, W.S.1
  • 7
    • 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 WS (1999) Conformational change in the pheromone-binding protein from Bombyx mori induced by pH and by interaction with membranes. J Biol Chem 274(43):30950-30956.
    • (1999) J Biol Chem , vol.274 , Issue.43 , pp. 30950-30956
    • Wojtasek, H.1    Leal, W.S.2
  • 8
    • 0034041910 scopus 로고    scopus 로고
    • NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori
    • Damberger F, et al. (2000) NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori. Protein Sci 9(5):1038-1041. (Pubitemid 30353347)
    • (2000) Protein Science , vol.9 , Issue.5 , pp. 1038-1041
    • Damberger, F.1    Nikonova, L.2    Horst, R.3    Peng, G.4    Leal, W.S.5    Wuthrich, K.6
  • 9
    • 0034141728 scopus 로고    scopus 로고
    • Sexual attraction in the silkworm moth: Structure of the pheromone-binding-protein-bombykol complex
    • DOI 10.1016/S1074-5521(00)00078-8
    • Sandler BH, Nikonova L, Leal WS, Clardy J (2000) Sexual attraction in the silkworm moth: Structure of the pheromone-binding-protein-bombykol complex. Chem Biol 7(2):143-151. (Pubitemid 30086840)
    • (2000) Chemistry and Biology , vol.7 , Issue.2 , pp. 143-151
    • Sandler, B.H.1    Nikonova, L.2    Leal, W.S.3    Clardy, J.4
  • 12
    • 0034605909 scopus 로고    scopus 로고
    • Analysis of the silkworm moth pheromone binding protein-pheromone complex by electrospray-ionization mass spectrometry
    • Oldham NJ, et al. (2000) Analysis of the silkworm moth pheromone binding protein-pheromone complex by electrospray-ionization mass spectrometry. Angew Chem Int Ed 39(23):4341-4343.
    • (2000) Angew Chem Int Ed , vol.39 , Issue.23 , pp. 4341-4343
    • Oldham, N.J.1
  • 13
    • 24044469677 scopus 로고    scopus 로고
    • Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein
    • Lautenschläger C, Leal WS, Clardy J (2005) Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein. Biochem Biophys Res Commun 335(4):1044-1050.
    • (2005) Biochem Biophys Res Commun , vol.335 , Issue.4 , pp. 1044-1050
    • Lautenschläger, C.1    Leal, W.S.2    Clardy, J.3
  • 14
    • 34848921468 scopus 로고    scopus 로고
    • Structural Basis of Ligand Binding and Release in Insect Pheromone-binding Proteins: NMR Structure of Antheraea polyphemus PBP1 at pH 4.5
    • DOI 10.1016/j.jmb.2007.07.078, PII S002228360701056X
    • Damberger FF, Ishida Y, Leal WS, Wüthrich K (2007) Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5. J Mol Biol 373(4):811-819. (Pubitemid 47498433)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.4 , pp. 811-819
    • Damberger, F.F.1    Ishida, Y.2    Leal, W.S.3    Wuthrich, K.4
  • 15
    • 70450270549 scopus 로고    scopus 로고
    • Ligand binding turns moth pheromone-binding protein into a pH sensor: Effect on the Antheraea polyphemus PBP1 conformation
    • Katre UV, Mazumder S, Prusti RK, Mohanty S (2009) Ligand binding turns moth pheromone-binding protein into a pH sensor: Effect on the Antheraea polyphemus PBP1 conformation. J Biol Chem 284(46):32167-32177.
    • (2009) J Biol Chem , vol.284 , Issue.46 , pp. 32167-32177
    • Katre, U.V.1    Mazumder, S.2    Prusti, R.K.3    Mohanty, S.4
  • 16
    • 79955484933 scopus 로고    scopus 로고
    • Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein
    • Michel E, et al. (2011) Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein. J Mol Biol 408(5):922-931.
    • (2011) J Mol Biol , vol.408 , Issue.5 , pp. 922-931
    • Michel, E.1
  • 17
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt A, Nielsen SO (1966) Hydrogen exchange in proteins. Adv Protein Chem 21:287-386.
    • (1966) Adv Protein Chem , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 21
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C (1970) Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv Protein Chem 24:1-95.
    • (1970) Adv Protein Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 22
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • Barrick D, Baldwin RL (1993) Three-state analysis of sperm whale apomyoglobin folding. Biochemistry 32(14):3790-3796. (Pubitemid 23126958)
    • (1993) Biochemistry , vol.32 , Issue.14 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 23
    • 0031038733 scopus 로고    scopus 로고
    • Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants
    • DOI 10.1021/bi9609681
    • Ionescu RM, Eftink MR (1997) Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants. Biochemistry 36(5):1129-1140. (Pubitemid 27076374)
    • (1997) Biochemistry , vol.36 , Issue.5 , pp. 1129-1140
    • Ionescu, R.M.1    Eftink, M.R.2
  • 24
    • 34548428720 scopus 로고    scopus 로고
    • Bombyx mori pheromone-binding protein binding nonpheromone ligands: Implications for pheromone recognition
    • Lautenschläger C, Leal WS, Clardy J (2007) Bombyx mori pheromone-binding protein binding nonpheromone ligands: Implications for pheromone recognition. Structure 15(9):1148-1154.
    • (2007) Structure , vol.15 , Issue.9 , pp. 1148-1154
    • Lautenschläger, C.1    Leal, W.S.2    Clardy, J.3
  • 25
    • 65649125608 scopus 로고    scopus 로고
    • Characterisation of Bombyx mori Odorant-binding proteins reveals that a general odorant-binding protein discriminates between sex pheromone components
    • Zhou JJ, et al. (2009) Characterisation of Bombyx mori Odorant-binding proteins reveals that a general odorant-binding protein discriminates between sex pheromone components. J Mol Biol 389(3):529-545.
    • (2009) J Mol Biol , vol.389 , Issue.3 , pp. 529-545
    • Zhou, J.J.1
  • 26
    • 84866029268 scopus 로고    scopus 로고
    • Specificity determinants of the silkworm moth sex pheromone
    • Xu P, Hooper AM, Pickett JA, Leal WS (2012) Specificity determinants of the silkworm moth sex pheromone. PLoS ONE 7(9):e44190.
    • (2012) PLoS ONE , vol.7 , Issue.9
    • Xu, P.1    Hooper, A.M.2    Pickett, J.A.3    Leal, W.S.4
  • 27
    • 0026702207 scopus 로고
    • Immunocytochemical localization of pheromone-binding protein in moth antennae
    • Steinbrecht RA, Ozaki M, Ziegelberger G (1992) Immunocytochemical localization of pheromone-binding protein in moth antennae. Cell Tissue Res 270(2):287-302.
    • (1992) Cell Tissue Res , vol.270 , Issue.2 , pp. 287-302
    • Steinbrecht, R.A.1    Ozaki, M.2    Ziegelberger, G.3
  • 28
    • 14844351843 scopus 로고    scopus 로고
    • Insect sex-pheromone signals mediated by specific combinations of olfactory receptors
    • DOI 10.1126/science.1106267
    • Nakagawa T, Sakurai T, Nishioka T, Touhara K (2005) Insect sex-pheromone signals mediated by specific combinations of olfactory receptors. Science 307(5715):1638-1642. (Pubitemid 40354748)
    • (2005) Science , vol.307 , Issue.5715 , pp. 1638-1642
    • Nakagawa, T.1    Sakurai, T.2    Nishioka, T.3    Touhara, K.4
  • 30
    • 42549164169 scopus 로고    scopus 로고
    • Insect olfactory receptors are heteromeric ligand-gated ion channels
    • DOI 10.1038/nature06850, PII NATURE06850
    • Sato K, et al. (2008) Insect olfactory receptors are heteromeric ligand-gated ion channels. Nature 452(7190):1002-1006. (Pubitemid 351589615)
    • (2008) Nature , vol.452 , Issue.7190 , pp. 1002-1006
    • Sato, K.1    Pellegrino, M.2    Nakagawa, T.3    Nakagawa, T.4    Vosshall, L.B.5    Touhara, K.6
  • 31
    • 0036864762 scopus 로고    scopus 로고
    • Moth pheromone binding proteins contribute to the excitation of olfactory receptor cells
    • Pophof B (2002) Moth pheromone binding proteins contribute to the excitation of olfactory receptor cells. Naturwissenschaften 89(11):515-518.
    • (2002) Naturwissenschaften , vol.89 , Issue.11 , pp. 515-518
    • Pophof, B.1
  • 32
    • 45449113774 scopus 로고    scopus 로고
    • Activation of Pheromone-Sensitive Neurons Is Mediated by Conformational Activation of Pheromone-Binding Protein
    • DOI 10.1016/j.cell.2008.04.046, PII S0092867408006375
    • Laughlin JD, Ha TS, Jones DN, Smith DP (2008) Activation of pheromone-sensitive neurons is mediated by conformational activation of pheromone-binding protein. Cell 133(7):1255-1265. (Pubitemid 351852909)
    • (2008) Cell , vol.133 , Issue.7 , pp. 1255-1265
    • Laughlin, J.D.1    Ha, T.S.2    Jones, D.N.M.3    Smith, D.P.4
  • 34
    • 0021712717 scopus 로고
    • Surface coats of pore tubules and olfactory sensory dendrites of a silkmoth revealed by cationic markers
    • Keil TA (1984) Surface coats of pore tubules and olfactory sensory dendrites of a silkmoth revealed by cationic markers. Tissue Cell 16(5):705-717.
    • (1984) Tissue Cell , vol.16 , Issue.5 , pp. 705-717
    • Keil, T.A.1
  • 35
    • 0025932041 scopus 로고
    • A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
    • van der Goot FG, González-Mañas JM, Lakey JH, Pattus F (1991) A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A. Nature 354(6352):408-410.
    • (1991) Nature , vol.354 , Issue.6352 , pp. 408-410
    • Van Der Goot, F.G.1    González-Mañas, J.M.2    Lakey, J.H.3    Pattus, F.4
  • 36
    • 0034673293 scopus 로고    scopus 로고
    • Duality monomer-dimer of the pheromone-binding protein from Bombyx mori
    • Leal WS (2000) Duality monomer-dimer of the pheromone-binding protein from Bombyx mori. Biochem Biophys Res Commun 268(2):521-529.
    • (2000) Biochem Biophys Res Commun , vol.268 , Issue.2 , pp. 521-529
    • Leal, W.S.1
  • 38
    • 77449092586 scopus 로고    scopus 로고
    • NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): Implications for pH-sensitive pheromone detection
    • Xu X, et al. (2010) NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): Implications for pH-sensitive pheromone detection. Biochemistry 49(7):1469-1476.
    • (2010) Biochemistry , vol.49 , Issue.7 , pp. 1469-1476
    • Xu, X.1
  • 39
    • 84873903213 scopus 로고    scopus 로고
    • Crystallographic observation of pH-induced conformational changes in the Amyelois transitella pheromone-binding protein AtraPBP1
    • di Luccio E, Ishida Y, Leal WS, Wilson DK (2013) Crystallographic observation of pH-induced conformational changes in the Amyelois transitella pheromone-binding protein AtraPBP1. PLoS ONE 8(2):e53840.
    • (2013) PLoS ONE , vol.8 , Issue.2
    • Di Luccio, E.1    Ishida, Y.2    Leal, W.S.3    Wilson, D.K.4
  • 40
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • Mori S, Abeygunawardana C, Johnson MO, van Zijl PC (1995) Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J Magn Reson B 108(1):94-98.
    • (1995) J Magn Reson B , vol.108 , Issue.1 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    Van Zijl, P.C.4
  • 41
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C, Xia TH, Billeter M, Güntert P, Wüthrich K (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomol NMR 6(1):1-10.
    • (1995) J Biomol NMR , vol.6 , Issue.1 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 43
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K (1996) MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graph 14(1):51-55, 29-32.
    • (1996) J Mol Graph , vol.14 , Issue.1
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 44
    • 70349896207 scopus 로고    scopus 로고
    • Olfactory perireceptor and receptor events in moths: A kinetic model revisited
    • Kaissling KE (2009) Olfactory perireceptor and receptor events in moths: a kinetic model revisited. J Comp Physiol A 195:895-922.
    • (2009) J Comp Physiol A , vol.195 , pp. 895-922
    • Kaissling, K.E.1
  • 45
    • 84885953811 scopus 로고    scopus 로고
    • Kinetics of olfactory responses might largely depend on the odorant-receptor interaction and the odorant deactivation postulated for flux detectors
    • 10.1007/s00359-013-0812-z
    • Kaissling KE (2013) Kinetics of olfactory responses might largely depend on the odorant-receptor interaction and the odorant deactivation postulated for flux detectors. J Comp A, 10.1007/s00359-013-0812-z.
    • (2013) J Comp A
    • Kaissling, K.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.