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Volumn 414, Issue 3, 2011, Pages 401-412

The crystal structure of odorant binding protein 7 from Anopheles gambiae exhibits an outstanding adaptability of its binding site

Author keywords

Anopheles gambiae; crystal structure; odorant binding protein; olfaction

Indexed keywords

DISULFIDE; INSECT PROTEIN; ODORANT BINDING PROTEIN 7; UNCLASSIFIED DRUG;

EID: 82555168318     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.10.005     Document Type: Article
Times cited : (77)

References (47)
  • 1
    • 0031389773 scopus 로고    scopus 로고
    • Elements of the olfactory signaling pathways in insect antennae
    • DOI 10.1007/BF02480368
    • Krieger J., Mameli M., and Breer H. Elements of the olfactory signaling pathways in insect antennae Invertebr. Neurosci. 3 1997 137 144 (Pubitemid 28433010)
    • (1997) Invertebrate Neuroscience , vol.3 , Issue.2-3 , pp. 137-144
    • Krieger, J.1    Mameli, M.2    Breer, H.3
  • 2
    • 0019489601 scopus 로고
    • Pheromone binding and inactivation by moth antennae
    • DOI 10.1038/293161a0
    • Vogt R.G., and Riddiford L.M. Pheromone binding and inactivation by moth antennae Nature 293 1981 161 163 (Pubitemid 11009908)
    • (1981) Nature , vol.293 , Issue.5828 , pp. 161-163
    • Vogt, R.G.1    Riddiford, L.M.2
  • 4
    • 34547668505 scopus 로고    scopus 로고
    • Molecular architecture of smell and taste in Drosophila
    • DOI 10.1146/annurev.neuro.30.051606.094306
    • Vosshall L.B., and Stocker R.F. Molecular architecture of smell and taste in Drosophila Annu. Rev. Neurosci. 30 2007 505 533 (Pubitemid 47218766)
    • (2007) Annual Review of Neuroscience , vol.30 , pp. 505-533
    • Vosshall, L.B.1    Stocker, R.F.2
  • 5
    • 42549164169 scopus 로고    scopus 로고
    • Insect olfactory receptors are heteromeric ligand-gated ion channels
    • DOI 10.1038/nature06850, PII NATURE06850
    • Sato K., Pellegrino M., Nakagawa T., Vosshall L.B., and Touhara K. Insect olfactory receptors are heteromeric ligand-gated ion channels Nature 452 2008 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
  • 6
    • 42549118499 scopus 로고    scopus 로고
    • Drosophila odorant receptors are both ligand-gated and cyclic-nucleotide- activated cation channels
    • DOI 10.1038/nature06861, PII NATURE06861
    • Wicher D., Schafer R., Bauernfeind R., Stensmyr M.C., Heller R., Heinemann S.H., and Hansson B.S. Drosophila odorant receptors are both ligand-gated and cyclic-nucleotide-activated cation channels Nature 452 2008 1007 1011 (Pubitemid 351589619)
    • (2008) Nature , vol.452 , Issue.7190 , pp. 1007-1011
    • Wicher, D.1    Schafer, R.2    Bauernfeind, R.3    Stensmyr, M.C.4    Heller, R.5    Heinemann, S.H.6    Hansson, B.S.7
  • 7
    • 0026721025 scopus 로고
    • Olfactory receptor neurons from antennae of developing male Manduca sexta respond to components of the species-specific sex pheromone in vitro
    • Stengl M., Zufall F., Hatt H., and Hildebrand J.G. Olfactory receptor neurons from antennae of developing male Manduca sexta respond to components of the species-specific sex pheromone in vitro J. Neurosci. 12 1992 2523 2531
    • (1992) J. Neurosci. , vol.12 , pp. 2523-2531
    • Stengl, M.1    Zufall, F.2    Hatt, H.3    Hildebrand, J.G.4
  • 8
    • 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 J.D., Ha T.S., Jones D.N., and Smith D.P. Activation of pheromone-sensitive neurons is mediated by conformational activation of pheromone-binding protein Cell 133 2008 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
  • 9
    • 77449111141 scopus 로고    scopus 로고
    • A receptor and binding protein interplay in the detection of a distinct pheromone component in the silkmoth Antheraea polyphemus
    • Forstner M., Breer H., and Krieger J. A receptor and binding protein interplay in the detection of a distinct pheromone component in the silkmoth Antheraea polyphemus Int. J. Biol. Sci. 5 2009 745 757
    • (2009) Int. J. Biol. Sci. , vol.5 , pp. 745-757
    • Forstner, M.1    Breer, H.2    Krieger, J.3
  • 10
    • 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 B.H., Nikonova L., Leal W.S., and Clardy J. Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex Chem. Biol. 7 2000 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
    • 0041819527 scopus 로고    scopus 로고
    • Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster
    • DOI 10.1038/nsb960
    • Kruse S.W., Zhao R., Smith D.P., and Jones D.N. Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster Nat. Struct. Biol. 10 2003 694 700 (Pubitemid 37052406)
    • (2003) Nature Structural Biology , vol.10 , Issue.9 , pp. 694-700
    • Kruse, S.W.1    Zhao, R.2    Smith, D.P.3    Jones, D.N.M.4
  • 14
    • 28144452847 scopus 로고    scopus 로고
    • The crystal structure of an odorant binding protein from Anopheles gambiae: Evidence for a common ligand release mechanism
    • DOI 10.1016/j.bbrc.2005.10.191, PII S0006291X05024368
    • Wogulis M., Morgan T., Ishida Y., Leal W.S., and Wilson D.K. The crystal structure of an odorant binding protein from Anopheles gambiae: evidence for a common ligand release mechanism Biochem. Biophys. Res. Commun. 339 2006 157 164 (Pubitemid 41697529)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.1 , pp. 157-164
    • Wogulis, M.1    Morgan, T.2    Ishida, Y.3    Leal, W.S.4    Wilson, D.K.5
  • 15
    • 0042029724 scopus 로고    scopus 로고
    • The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism
    • DOI 10.1074/jbc.M304688200
    • Lartigue A., Gruez A., Spinelli S., Riviere S., Brossut R., Tegoni M., and Cambillau C. The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism J. Biol. Chem. 278 2003 30213 30218 (Pubitemid 36962415)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 30213-30218
    • Lartigue, A.1    Gruez, A.2    Spinelli, S.3    Riviere, S.4    Brossut, R.5    Tegoni, M.6    Cambillau, C.7
  • 16
    • 64849108031 scopus 로고    scopus 로고
    • Structural basis of the broad specificity of a general odorant-binding protein from honeybee
    • Lescop E., Briand L., Pernollet J.C., and Guittet E. Structural basis of the broad specificity of a general odorant-binding protein from honeybee Biochemistry 48 2009 2431 2441
    • (2009) Biochemistry , vol.48 , pp. 2431-2441
    • Lescop, E.1    Briand, L.2    Pernollet, J.C.3    Guittet, E.4
  • 17
    • 2342617588 scopus 로고    scopus 로고
    • Structural aspects of sexual attraction and chemical communication in insects
    • DOI 10.1016/j.tibs.2004.03.003, PII S0968000404000714
    • Tegoni M., Campanacci V., and Cambillau C. Structural aspects of sexual attraction and chemical communication in insects Trends Biochem. Sci. 29 2004 257 264 (Pubitemid 38591320)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.5 , pp. 257-264
    • Tegoni, M.1    Campanacci, V.2    Cambillau, C.3
  • 18
    • 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
  • 19
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • DOI 10.1093/nar/gkg556
    • Gouet P., Robert X., and Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins Nucleic Acids Res. 31 2003 3320 3323 (Pubitemid 37442149)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 20
    • 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 F.F., Ishida Y., Leal W.S., and Wuthrich K. 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 2007 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
  • 23
    • 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 J.J., Robertson G., He X., Dufour S., Hooper A.M., and Pickett J.A. Characterisation of Bombyx mori odorant-binding proteins reveals that a general odorant-binding protein discriminates between sex pheromone components J. Mol. Biol. 389 2009 529 545
    • (2009) J. Mol. Biol. , vol.389 , pp. 529-545
    • Zhou, J.J.1    Robertson, G.2    He, X.3    Dufour, S.4    Hooper, A.M.5    Pickett, J.A.6
  • 25
    • 33750502864 scopus 로고    scopus 로고
    • Function and evolution of a gene family encoding odorant binding-like proteins in a social insect, the honey bee (Apis mellifera)
    • DOI 10.1101/gr.5075706
    • Foret S., and Maleszka R. Function and evolution of a gene family encoding odorant binding-like proteins in a social insect, the honey bee (Apis mellifera) Genome Res. 16 2006 1404 1413 (Pubitemid 44664683)
    • (2006) Genome Research , vol.16 , Issue.11 , pp. 1404-1413
    • Foret, S.1    Maleszka, R.2
  • 26
    • 83055176313 scopus 로고    scopus 로고
    • Crystal structure of Apis mellifera OBP 14, a C-minus odorant-binding protein, and its complexes with odorant molecules
    • doi:10.1016/j.ibmb.2011.10.005 In press
    • Spinelli, S., Lagarde, L., Iovinella, I., Legrand, P., Tegoni, M., Pelosi, P. and Cambillau, C. Crystal structure of Apis mellifera OBP 14, a C-minus odorant-binding protein, and its complexes with odorant molecules. Insect Biochem. Mol. Biol. In press. doi:10.1016/j.ibmb.2011.10.005.
    • Insect Biochem. Mol. Biol.
    • Spinelli, S.1    Lagarde, L.2    Iovinella, I.3    Legrand, P.4    Tegoni, M.5    Pelosi, P.6    Cambillau, C.7
  • 27
    • 0442323553 scopus 로고    scopus 로고
    • "Plus-C" odorant-binding protein genes in two Drosophila species and the malaria mosquito Anopheles gambiae
    • DOI 10.1016/j.gene.2003.11.007
    • Zhou J.J., Huang W., Zhang G.A., Pickett J.A., and Field L.M. "Plus-C" odorant-binding protein genes in two Drosophila species and the malaria mosquito Anopheles gambiae Gene 327 2004 117 129 (Pubitemid 38186654)
    • (2004) Gene , vol.327 , Issue.1 , pp. 117-129
    • Zhou, J.-J.1    Huang, W.2    Zhang, G.-A.3    Pickett, J.A.4    Field, L.M.5
  • 28
    • 79960219821 scopus 로고    scopus 로고
    • Crystal structure of a novel type of odorant binding protein from Anopheles gambiae, belonging to the C+ class
    • Lagarde A., Spinelli S., Qiao H., Tegoni M., Pelosi P., and Cambillau C. Crystal structure of a novel type of odorant binding protein from Anopheles gambiae, belonging to the C+ class Biochem. J. 437 2011 423 430
    • (2011) Biochem. J. , vol.437 , pp. 423-430
    • Lagarde, A.1    Spinelli, S.2    Qiao, H.3    Tegoni, M.4    Pelosi, P.5    Cambillau, C.6
  • 29
    • 0036740299 scopus 로고    scopus 로고
    • Genome-wide analysis of the odorant-binding protein gene family in Drosophila melanogaster
    • Hekmat-Scafe D.S., Scafe C.R., McKinney A.J., and Tanouye M.A. Genome-wide analysis of the odorant-binding protein gene family in Drosophila melanogaster Genome Res. 12 2002 1357 1369
    • (2002) Genome Res. , vol.12 , pp. 1357-1369
    • Hekmat-Scafe, D.S.1    Scafe, C.R.2    McKinney, A.J.3    Tanouye, M.A.4
  • 30
    • 62649119139 scopus 로고    scopus 로고
    • Multifunctionality and mechanism of ligand binding in a mosquito antiinflamatory protein
    • Calvo E., Mans B.J., Ribeiro J.M.C., and Andersen J.F. Multifunctionality and mechanism of ligand binding in a mosquito antiinflamatory protein Proc. Natl Acad. Sci. USA 106 2009 3728 3733
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 3728-3733
    • Calvo, E.1    Mans, B.J.2    Ribeiro, J.M.C.3    Andersen, J.F.4
  • 31
    • 0034960584 scopus 로고    scopus 로고
    • Detection and removal of an artefact fatty acid from the binding site of recombinant Bombyx mori pheromone-binding protein
    • Oldham N.J., Krieger J., Breer H., and Svatos A. Detection and removal of an artefact fatty acid from the binding site of recombinant Bombyx mori pheromone-binding protein Chem. Senses 26 2001 529 531 (Pubitemid 32600181)
    • (2001) Chemical Senses , vol.26 , Issue.5 , pp. 529-531
    • Oldham, N.J.1    Krieger, J.2    Breer, H.3    Svatos, A.4
  • 32
    • 79958718246 scopus 로고    scopus 로고
    • Cooperative interactions between odorant-binding proteins of Anopheles gambiae
    • Qiao H., He X., Schymura D., Ban L., Field L., and Dani F.R. Cooperative interactions between odorant-binding proteins of Anopheles gambiae Cell. Mol. Life Sci. 68 2011 1799 1813
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1799-1813
    • Qiao, H.1    He, X.2    Schymura, D.3    Ban, L.4    Field, L.5    Dani, F.R.6
  • 33
    • 77949743740 scopus 로고    scopus 로고
    • The Anopheles gambiae odorant binding protein 1 (AgamOBP1) mediates indole recognition in the antennae of female mosquitoes
    • Biessmann H., Andronopoulou E., Biessmann M.R., Douris V., Dimitratos S.D., and Eliopoulos E. The Anopheles gambiae odorant binding protein 1 (AgamOBP1) mediates indole recognition in the antennae of female mosquitoes PLoS One 5 2010 e9471
    • (2010) PLoS One , vol.5 , pp. 9471
    • Biessmann, H.1    Andronopoulou, E.2    Biessmann, M.R.3    Douris, V.4    Dimitratos, S.D.5    Eliopoulos, E.6
  • 34
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 35
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • DOI 10.1093/nar/gkl282
    • Dundas J., Ouyang Z., Tseng J., Binkowski A., Turpaz Y., and Liang J. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues Nucleic Acids Res. 34 2006 W116 W118 (Pubitemid 44529746)
    • (2006) Nucleic Acids Research , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 36
    • 24044469677 scopus 로고    scopus 로고
    • Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein
    • DOI 10.1016/j.bbrc.2005.07.176, PII S0006291X05016311
    • Lautenschlager C., Leal W.S., and Clardy J. Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein Biochem. Biophys. Res. Commun. 335 2005 1044 1050 (Pubitemid 41215524)
    • (2005) Biochemical and Biophysical Research Communications , vol.335 , Issue.4 , pp. 1044-1050
    • Lautenschlager, C.1    Leal, W.S.2    Clardy, J.3
  • 37
    • 34548428720 scopus 로고    scopus 로고
    • Bombyx mori Pheromone-Binding Protein Binding Nonpheromone Ligands: Implications for Pheromone Recognition
    • DOI 10.1016/j.str.2007.07.013, PII S0969212607002869
    • Lautenschlager C., Leal W.S., and Clardy J. Bombyx mori pheromone-binding protein binding nonpheromone ligands: implications for pheromone recognition Structure 15 2007 1148 1154 (Pubitemid 47362693)
    • (2007) Structure , vol.15 , Issue.9 , pp. 1148-1154
    • Lautenschlager, C.1    Leal, W.S.2    Clardy, J.3
  • 38
    • 63149188087 scopus 로고    scopus 로고
    • Production and biophysical characterization of the CorA transporter from Methanosarcina mazei
    • Veesler D., Blangy S., Siponen M., Vincentelli R., Cambillau C., and Sciara G. Production and biophysical characterization of the CorA transporter from Methanosarcina mazei Anal. Biochem. 388 2009 115 121
    • (2009) Anal. Biochem. , vol.388 , pp. 115-121
    • Veesler, D.1    Blangy, S.2    Siponen, M.3    Vincentelli, R.4    Cambillau, C.5    Sciara, G.6
  • 40
    • 0037507302 scopus 로고    scopus 로고
    • Optimization of crystals from nanodrops: Crystallization and preliminary crystallographic study of a pheromone-binding protein from the honeybee Apis mellifera L
    • DOI 10.1107/S090744490300413X
    • Lartigue A., Gruez A., Briand L., Pernollet J.C., Spinelli S., Tegoni M., and Cambillau C. Optimization of crystals from nanodrops: crystallization and preliminary crystallographic study of a pheromone-binding protein from the honeybee Apis mellifera L Acta Crystallogr., Sect. D: Biol. Crystallogr. 59 2003 919 921 (Pubitemid 36599374)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.5 , pp. 919-921
    • Lartigue, A.1    Gruez, A.2    Briand, L.3    Pernollet, J.-C.4    Spinelli, S.5    Tegoni, M.6    Cambillau, C.7
  • 42
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin A., and Teplyakov A. MOLREP: an Automated Program for Molecular Replacement J. Appl. Crystallogr. 30 1997 1022 1025 (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2


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