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Volumn 481, Issue 1-2, 2016, Pages 146-152

Crystal structure of Arabidopsis thaliana SNC1 TIR domain

Author keywords

Dimerization; Immunity; Plant

Indexed keywords

PROTEIN; SUPPRESSOR OF NPR1 1 CONSTITUTIVE 1; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; PROTEIN BINDING; SNC1 PROTEIN, ARABIDOPSIS;

EID: 85001132606     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2016.11.004     Document Type: Article
Times cited : (19)

References (23)
  • 1
    • 0142057020 scopus 로고    scopus 로고
    • Understanding the functions of plant disease resistance proteins
    • [1] Martin, G.B., Bogdanove, A.J., Sessa, G., Understanding the functions of plant disease resistance proteins. Annu. Rev. Plant Biol. 54 (2003), 23–61.
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 23-61
    • Martin, G.B.1    Bogdanove, A.J.2    Sessa, G.3
  • 2
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • [2] Jones, J.D., Dangl, J.L., The plant immune system. Nature 444 (2006), 323–329.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 3
    • 84938699156 scopus 로고    scopus 로고
    • Understanding plant immunity as a surveillance system to detect invasion
    • [3] Cook, D.E., Mesarich, C.H., Thomma, B.P., Understanding plant immunity as a surveillance system to detect invasion. Annu. Rev. Phytopathol. 53 (2015), 541–563.
    • (2015) Annu. Rev. Phytopathol. , vol.53 , pp. 541-563
    • Cook, D.E.1    Mesarich, C.H.2    Thomma, B.P.3
  • 4
    • 84928897756 scopus 로고    scopus 로고
    • Effector-triggered immunity: from pathogen perception to robust defense
    • [4] Cui, H., Tsuda, K., Parker, J.E., Effector-triggered immunity: from pathogen perception to robust defense. Annu. Rev. Plant Biol. 66 (2015), 487–511.
    • (2015) Annu. Rev. Plant Biol. , vol.66 , pp. 487-511
    • Cui, H.1    Tsuda, K.2    Parker, J.E.3
  • 5
    • 84987779504 scopus 로고    scopus 로고
    • Recent advances in plant NLR structure, function, localization, and signaling
    • [5] Qi, D., Innes, R.W., Recent advances in plant NLR structure, function, localization, and signaling. Front. Immunol., 4, 2013, 348.
    • (2013) Front. Immunol. , vol.4 , pp. 348
    • Qi, D.1    Innes, R.W.2
  • 8
    • 34548459012 scopus 로고    scopus 로고
    • Mammalian NLR proteins; discriminating foe from friend
    • [8] Kaparakis, M., Philpott, D.J., Ferrero, R.L., Mammalian NLR proteins; discriminating foe from friend. Immunol. Cell Biol. 85 (2007), 495–502.
    • (2007) Immunol. Cell Biol. , vol.85 , pp. 495-502
    • Kaparakis, M.1    Philpott, D.J.2    Ferrero, R.L.3
  • 9
    • 84859346744 scopus 로고    scopus 로고
    • Structure-function analysis of the coiled-coil and leucine-rich repeat domains of the RPS5 disease resistance protein
    • [9] Qi, D., DeYoung, B.J., Innes, R.W., Structure-function analysis of the coiled-coil and leucine-rich repeat domains of the RPS5 disease resistance protein. Plant Physiol. 158 (2012), 1819–1832.
    • (2012) Plant Physiol. , vol.158 , pp. 1819-1832
    • Qi, D.1    DeYoung, B.J.2    Innes, R.W.3
  • 11
    • 84924405788 scopus 로고    scopus 로고
    • Molecular and functional analyses of a maize autoactive NB-LRR protein identify precise structural requirements for activity
    • [11] Wang, G.F., Ji, J., El-Kasmi, F., Dangl, J.L., Johal, G., Balint-Kurti, P.J., Molecular and functional analyses of a maize autoactive NB-LRR protein identify precise structural requirements for activity. PLoS Pathog., 11, 2015, e1004674.
    • (2015) PLoS Pathog. , vol.11 , pp. e1004674
    • Wang, G.F.1    Ji, J.2    El-Kasmi, F.3    Dangl, J.L.4    Johal, G.5    Balint-Kurti, P.J.6
  • 12
    • 84864511877 scopus 로고    scopus 로고
    • How to build a pathogen detector: structural basis of NB-LRR function
    • [12] Takken, F.L., Goverse, A., How to build a pathogen detector: structural basis of NB-LRR function. Curr. Opin. Plant Biol. 15 (2012), 375–384.
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 375-384
    • Takken, F.L.1    Goverse, A.2
  • 13
    • 79952643473 scopus 로고    scopus 로고
    • Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation
    • [13] Bernoux, M., Ve, T., Williams, S., Warren, C., Hatters, D., Valkov, E., Zhang, X., Ellis, J.G., Kobe, B., Dodds, P.N., Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation. Cell Host Microbe 9 (2011), 200–211.
    • (2011) Cell Host Microbe , vol.9 , pp. 200-211
    • Bernoux, M.1    Ve, T.2    Williams, S.3    Warren, C.4    Hatters, D.5    Valkov, E.6    Zhang, X.7    Ellis, J.G.8    Kobe, B.9    Dodds, P.N.10
  • 14
    • 79960505285 scopus 로고    scopus 로고
    • Cell death mediated by the N-terminal domains of a unique and highly conserved class of NB-LRR protein
    • [14] Collier, S.M., Hamel, L.P., Moffett, P., Cell death mediated by the N-terminal domains of a unique and highly conserved class of NB-LRR protein. Mol. Plant Microbe Interact. 24 (2011), 918–931.
    • (2011) Mol. Plant Microbe Interact. , vol.24 , pp. 918-931
    • Collier, S.M.1    Hamel, L.P.2    Moffett, P.3
  • 15
    • 59749083228 scopus 로고    scopus 로고
    • The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction
    • [15] Swiderski, M.R., Birker, D., Jones, J.D., The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction. Mol. Plant Microbe Interact. 22 (2009), 157–165.
    • (2009) Mol. Plant Microbe Interact. , vol.22 , pp. 157-165
    • Swiderski, M.R.1    Birker, D.2    Jones, J.D.3
  • 16
    • 84925486323 scopus 로고    scopus 로고
    • Toll/interleukin-1 receptor (TIR) domain-mediated cellular signaling pathways
    • [16] Narayanan, K.B., Park, H.H., Toll/interleukin-1 receptor (TIR) domain-mediated cellular signaling pathways. Apoptosis 20 (2015), 196–209.
    • (2015) Apoptosis , vol.20 , pp. 196-209
    • Narayanan, K.B.1    Park, H.H.2
  • 17
    • 84925465183 scopus 로고    scopus 로고
    • Structure and function of Toll/interleukin-1 receptor/resistance protein (TIR) domains
    • [17] Ve, T., Williams, S.J., Kobe, B., Structure and function of Toll/interleukin-1 receptor/resistance protein (TIR) domains. Apoptosis 20 (2015), 250–261.
    • (2015) Apoptosis , vol.20 , pp. 250-261
    • Ve, T.1    Williams, S.J.2    Kobe, B.3
  • 19
    • 75149175757 scopus 로고    scopus 로고
    • The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants
    • [19] Chan, S.L., Mukasa, T., Santelli, E., Low, L.Y., Pascual, J., The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants. Protein Sci. 19 (2010), 155–161.
    • (2010) Protein Sci. , vol.19 , pp. 155-161
    • Chan, S.L.1    Mukasa, T.2    Santelli, E.3    Low, L.Y.4    Pascual, J.5
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Minor W processing of X-ray diffraction data collected in oscillation mode
    • [20] Otwinowski, Z., Minor W processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystall 276:Pt A (1997), 307–326.
    • (1997) Macromol. Crystall , vol.276 , pp. 307-326
    • Otwinowski, Z.1
  • 21
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive python-based system for macromolecular structure solution
    • [21] Adams, P.D., et al. PHENIX: a comprehensive python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66:Pt 2 (2010), 213–221.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 23
    • 0344945644 scopus 로고    scopus 로고
    • A gain-of-function mutation in a plant disease resistance gene leads to constitutive activation of downstream signal transduction pathways in suppressor of npr1-1, constitutive 1
    • [23] Zhang, Y., Goritschnig, S., Dong, X., Li, X., A gain-of-function mutation in a plant disease resistance gene leads to constitutive activation of downstream signal transduction pathways in suppressor of npr1-1, constitutive 1. Plant Cell. 15 (2003), 2636–2646.
    • (2003) Plant Cell. , vol.15 , pp. 2636-2646
    • Zhang, Y.1    Goritschnig, S.2    Dong, X.3    Li, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.