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Volumn 7, Issue 9, 2012, Pages

Crystal Structure of Der f 7, a Dust Mite Allergen from Dermatophagoides farinae

Author keywords

[No Author keywords available]

Indexed keywords

DER F 7 ALLERGEN; DER P 7 ALLERGEN; HOUSE DUST ALLERGEN; IMMUNOGLOBULIN E; MONOCLONAL ANTIBODY; POLYMYXIN B; UNCLASSIFIED DRUG;

EID: 84866065833     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044850     Document Type: Article
Times cited : (22)

References (37)
  • 1
    • 0027141028 scopus 로고
    • Molecular cloning of a house dust mite allergen with common antibody binding specificities with multiple components in mite extracts
    • Shen HD, Chua KY, Lin KL, Hsieh KH, Thomas WR, (1993) Molecular cloning of a house dust mite allergen with common antibody binding specificities with multiple components in mite extracts. Clin Exp Allergy 23: 934-940.
    • (1993) Clin Exp Allergy , vol.23 , pp. 934-940
    • Shen, H.D.1    Chua, K.Y.2    Lin, K.L.3    Hsieh, K.H.4    Thomas, W.R.5
  • 2
    • 79951793841 scopus 로고    scopus 로고
    • Mite component-specific IgE repertoire and phenotypes of allergic disease in childhood: the tropical perspective
    • Kidon MI, Chiang WC, Liew WK, Ong TC, Tiong YS, et al. (2011) Mite component-specific IgE repertoire and phenotypes of allergic disease in childhood: the tropical perspective. Pediatr Allergy Immunol 22: 202-210.
    • (2011) Pediatr Allergy Immunol , vol.22 , pp. 202-210
    • Kidon, M.I.1    Chiang, W.C.2    Liew, W.K.3    Ong, T.C.4    Tiong, Y.S.5
  • 3
    • 77950301322 scopus 로고    scopus 로고
    • The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins
    • Mueller GA, Edwards LL, Aloor JJ, Fessler MB, Glesner J, et al. (2010) The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins. J Allergy Clin Immunol 125: 909-917.
    • (2010) J Allergy Clin Immunol , vol.125 , pp. 909-917
    • Mueller, G.A.1    Edwards, L.L.2    Aloor, J.J.3    Fessler, M.B.4    Glesner, J.5
  • 4
    • 0037069747 scopus 로고    scopus 로고
    • The BSP30 salivary proteins from cattle, LUNX/PLUNC and von Ebner's minor salivary gland protein are members of the PSP/LBP superfamily of proteins
    • Wheeler TT, Haigh BJ, McCracken JY, Wilkins RJ, Morris CA, et al. (2002) The BSP30 salivary proteins from cattle, LUNX/PLUNC and von Ebner's minor salivary gland protein are members of the PSP/LBP superfamily of proteins. Biochim Biophys Acta 1579: 92-100.
    • (2002) Biochim Biophys Acta , vol.1579 , pp. 92-100
    • Wheeler, T.T.1    Haigh, B.J.2    McCracken, J.Y.3    Wilkins, R.J.4    Morris, C.A.5
  • 5
    • 0028973133 scopus 로고
    • Molecular cloning and immunological characterization of the house dust mite allergen Der f 7
    • Shen H-D, Chua K-Y, Lin W-L, Hsieh K-H, Thomas WR, (1995) Molecular cloning and immunological characterization of the house dust mite allergen Der f 7. Clin Exp Allergy 25: 1000-1006.
    • (1995) Clin Exp Allergy , vol.25 , pp. 1000-1006
    • Shen, H.-D.1    Chua, K.-Y.2    Lin, W.-L.3    Hsieh, K.-H.4    Thomas, W.R.5
  • 6
    • 0030834372 scopus 로고    scopus 로고
    • Characterization of the allergen Der f 7 from house dust mite extracts by species-specific and crossreactive monoclonal antibodies
    • Shen HD, Lin WL, Tsai LC, Tam MF, Chua KY, et al. (1997) Characterization of the allergen Der f 7 from house dust mite extracts by species-specific and crossreactive monoclonal antibodies. Clin Exp Allergy 27: 824-832.
    • (1997) Clin Exp Allergy , vol.27 , pp. 824-832
    • Shen, H.D.1    Lin, W.L.2    Tsai, L.C.3    Tam, M.F.4    Chua, K.Y.5
  • 8
    • 77956480854 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of Der f 7, an allergen of Dermatophagoides farinae from China
    • Cui Y-B, Cai H-X, Zhou Y, Gao C-X, Shi W-H, et al. (2010) Cloning, expression, and characterization of Der f 7, an allergen of Dermatophagoides farinae from China. J Med Entomol 47: 868-876.
    • (2010) J Med Entomol , vol.47 , pp. 868-876
    • Cui, Y.-B.1    Cai, H.-X.2    Zhou, Y.3    Gao, C.-X.4    Shi, W.-H.5
  • 9
    • 79951942316 scopus 로고    scopus 로고
    • Homology modeling and monoclonal antibody binding of the Der f 7 dust mite allergen
    • Shen H-D, Tam MF, Huang C-H, Chou H, Tai H-Y, et al. (2011) Homology modeling and monoclonal antibody binding of the Der f 7 dust mite allergen. Immunol Cell Biol 89: 225-230.
    • (2011) Immunol Cell Biol , vol.89 , pp. 225-230
    • Shen, H.-D.1    Tam, M.F.2    Huang, C.-H.3    Chou, H.4    Tai, H.-Y.5
  • 10
    • 80051931126 scopus 로고    scopus 로고
    • Asp159 is a critical core amino acid of an IgE-binding and cross-reactive epitope of a dust mite allergen Der f 7
    • Chou H, Tam MF, Lee S-S, Tang R-B, Lin T-H, et al. (2011) Asp159 is a critical core amino acid of an IgE-binding and cross-reactive epitope of a dust mite allergen Der f 7. Mol Immunol 48: 2130-2134.
    • (2011) Mol Immunol , vol.48 , pp. 2130-2134
    • Chou, H.1    Tam, M.F.2    Lee, S.-S.3    Tang, R.-B.4    Lin, T.-H.5
  • 11
    • 40649091053 scopus 로고    scopus 로고
    • Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins
    • Kolodziejczyk R, Bujacz G, Jakób M, Ożyhar A, Jaskolski M, et al. (2008) Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins. J Mol Biol 377: 870-881.
    • (2008) J Mol Biol , vol.377 , pp. 870-881
    • Kolodziejczyk, R.1    Bujacz, G.2    Jakób, M.3    Ozyhar, A.4    Jaskolski, M.5
  • 12
    • 0030760314 scopus 로고    scopus 로고
    • Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution
    • Beamer LJ, Carroll SF, Eisenberg D, (1997) Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. Science 276: 1861-1864.
    • (1997) Science , vol.276 , pp. 1861-1864
    • Beamer, L.J.1    Carroll, S.F.2    Eisenberg, D.3
  • 13
    • 0034674059 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold
    • Kleiger G, Beamer LJ, Grothe R, Mallick P, Eisenberg D, (2000) The 1.7 Å crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold. J Mol Biol 299: 1019-1034.
    • (2000) J Mol Biol , vol.299 , pp. 1019-1034
    • Kleiger, G.1    Beamer, L.J.2    Grothe, R.3    Mallick, P.4    Eisenberg, D.5
  • 14
    • 63649118181 scopus 로고    scopus 로고
    • Crystal structure of Epiphyas postvittana Takeout 1 with bound ubiquinone supports a role as ligand carriers for takeout proteins in insects
    • Hamiaux C, Stanley D, Greenwood DR, Baker EN, Newcomb RD, (2009) Crystal structure of Epiphyas postvittana Takeout 1 with bound ubiquinone supports a role as ligand carriers for takeout proteins in insects. J Biol Chem 284: 3496-3503.
    • (2009) J Biol Chem , vol.284 , pp. 3496-3503
    • Hamiaux, C.1    Stanley, D.2    Greenwood, D.R.3    Baker, E.N.4    Newcomb, R.D.5
  • 15
    • 33846989758 scopus 로고    scopus 로고
    • Crystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid molecules
    • Qiu X, Mistry A, Ammirati MJ, Chrunyk BA, Clark RW, et al. (2007) Crystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid molecules. Nat Struct Mol Biol 14: 106-113.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 106-113
    • Qiu, X.1    Mistry, A.2    Ammirati, M.J.3    Chrunyk, B.A.4    Clark, R.W.5
  • 16
    • 0025196807 scopus 로고
    • Effects of five insect growth regulators on laboratory populations of the North American house-dust mite, Dermatophagoides farinae
    • Downing AS, Wright CG, Farrier MH, (1990) Effects of five insect growth regulators on laboratory populations of the North American house-dust mite, Dermatophagoides farinae. Exp Appl Acarol 9: 123-130.
    • (1990) Exp Appl Acarol , vol.9 , pp. 123-130
    • Downing, A.S.1    Wright, C.G.2    Farrier, M.H.3
  • 17
    • 0037091061 scopus 로고    scopus 로고
    • PLUNC: a novel family of candidate host defence proteins expressed in the upper airways and nasopharynx
    • Bingle CD, Craven CJ, (2002) PLUNC: a novel family of candidate host defence proteins expressed in the upper airways and nasopharynx. Hum Mol Genet 11: 937-943.
    • (2002) Hum Mol Genet , vol.11 , pp. 937-943
    • Bingle, C.D.1    Craven, C.J.2
  • 18
    • 0032007337 scopus 로고    scopus 로고
    • Role of the bactericidal/permeability-increasing protein in host defence
    • Elsbach P, Weiss J, (1998) Role of the bactericidal/permeability-increasing protein in host defence. Curr Opin Immunol 10: 45-49.
    • (1998) Curr Opin Immunol , vol.10 , pp. 45-49
    • Elsbach, P.1    Weiss, J.2
  • 19
    • 33846682753 scopus 로고    scopus 로고
    • Polymyxin B as inhibitor of LPS contamination of Schistosoma mansoni recombinant proteins in human cytokine analysis
    • Cardoso LS, Araujo MI, Góes AM, Pacífico LG, Oliveira RR, et al. (2007) Polymyxin B as inhibitor of LPS contamination of Schistosoma mansoni recombinant proteins in human cytokine analysis. Microb Cell Fact 6: 1.
    • (2007) Microb Cell Fact , vol.6 , pp. 1
    • Cardoso, L.S.1    Araujo, M.I.2    Góes, A.M.3    Pacífico, L.G.4    Oliveira, R.R.5
  • 20
    • 70349849656 scopus 로고    scopus 로고
    • Regulation of female reproduction in mites: A unifying model for the Acari
    • Cabrere AR, Donohue KV, Roe RM, (2009) Regulation of female reproduction in mites: A unifying model for the Acari. J Insect Physiol 55: 1079-1090.
    • (2009) J Insect Physiol , vol.55 , pp. 1079-1090
    • Cabrere, A.R.1    Donohue, K.V.2    Roe, R.M.3
  • 21
    • 0031913980 scopus 로고    scopus 로고
    • New insecticides with ecdysteroidal and juvenile hormone activity
    • Dhadialla TS, Carlson GR, Le DP, (1998) New insecticides with ecdysteroidal and juvenile hormone activity. Annu Rev Entomol 43: 545-569.
    • (1998) Annu Rev Entomol , vol.43 , pp. 545-569
    • Dhadialla, T.S.1    Carlson, G.R.2    Le, D.P.3
  • 22
    • 83055169811 scopus 로고    scopus 로고
    • Cloning, expresion, purification, crystallization and preliminary X-ray diffraction studies of a major group 7 allergen, Der f 7, from the dust mite Dermatophagoides farinae
    • Tan KW, Kumar S, Chew FT, Mok YK, (2011) Cloning, expresion, purification, crystallization and preliminary X-ray diffraction studies of a major group 7 allergen, Der f 7, from the dust mite Dermatophagoides farinae. Acta Crystallogr F 67: 1612-1615.
    • (2011) Acta Crystallogr F , vol.67 , pp. 1612-1615
    • Tan, K.W.1    Kumar, S.2    Chew, F.T.3    Mok, Y.K.4
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D 60: 2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 26
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive Python-based system for macromolecular structure solution
    • Adams PD, Afonine PV, Bunkóczi G, Chen VB, Davis IW, et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D 66: 213-221.
    • (2010) Acta Crystallogr D , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkóczi, G.3    Chen, V.B.4    Davis, I.W.5
  • 27
    • 0028904072 scopus 로고
    • Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2)
    • Ruiz-Sanz J, de Prat Gay G, Otzen DE, Fersht AR, (1995) Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2). Biochemistry 34: 1695-1701.
    • (1995) Biochemistry , vol.34 , pp. 1695-1701
    • Ruiz-Sanz, J.1    de Prat Gay, G.2    Otzen, D.E.3    Fersht, A.R.4
  • 28
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 29
    • 84875264931 scopus 로고    scopus 로고
    • SPARKY 3. University of California, San Francisco
    • Goddard TD, Kneller DG SPARKY 3. University of California, San Francisco.
    • Goddard, T.D.1    Kneller, D.G.2
  • 30
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the a- and b-carbon resonances in proteins
    • Wittekind M, Mueller L, (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the a- and b-carbon resonances in proteins. J Magn Reson B101: 201-205.
    • (1993) J Magn Reson , vol.B101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 31
    • 0027569483 scopus 로고
    • Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins
    • Grzesiek S, Bax A, (1993) Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. J Biomol NMR 3: 185-204.
    • (1993) J Biomol NMR , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 32
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0029881007 scopus 로고    scopus 로고
    • Molmol: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wϋthrich K, (1996) Molmol: A program for display and analysis of macromolecular structures. J Mol Graphics 14: 51-55.
    • (1996) J Mol Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wthrich, K.3
  • 35
    • 40749148575 scopus 로고    scopus 로고
    • On distance and similarity in fold space
    • Sippl MJ, (2008) On distance and similarity in fold space. Bioinformatics 24: 872-873.
    • (2008) Bioinformatics , vol.24 , pp. 872-873
    • Sippl, M.J.1
  • 36
    • 38849092210 scopus 로고    scopus 로고
    • A note on difficult structure alignment problems
    • Sippl MJ, Wiederstein M, (2008) A note on difficult structure alignment problems. Bioinformatics 24: 426-427.
    • (2008) Bioinformatics , vol.24 , pp. 426-427
    • Sippl, M.J.1    Wiederstein, M.2


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