메뉴 건너뛰기




Volumn 8, Issue 7, 2013, Pages

Three-Dimensional Structure of Human NLRP10/PYNOD Pyrin Domain Reveals a Homotypic Interaction Site Distinct from Its Mouse Homologue

Author keywords

[No Author keywords available]

Indexed keywords

PATTERN RECOGNITION RECEPTOR; PROTEIN NLRP10; UNCLASSIFIED DRUG;

EID: 84879816463     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0067843     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 60749104683 scopus 로고    scopus 로고
    • The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis
    • Franchi L, Eigenbrod T, Munoz-Planillo R, Nunez G, (2009) The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis. Nat Immunol 10: 241-247.
    • (2009) Nat Immunol , vol.10 , pp. 241-247
    • Franchi, L.1    Eigenbrod, T.2    Munoz-Planillo, R.3    Nunez, G.4
  • 3
    • 0035524488 scopus 로고    scopus 로고
    • Toll-like receptors and innate immunity
    • Medzhitov R, (2001) Toll-like receptors and innate immunity. Nat Rev Immunol 1: 135-145.
    • (2001) Nat Rev Immunol , vol.1 , pp. 135-145
    • Medzhitov, R.1
  • 4
    • 82955249021 scopus 로고    scopus 로고
    • NOD-like receptors and the innate immune system: coping with danger, damage and death
    • Kersse K, Bertrand MJ, Lamkanfi M, Vandenabeele P, (2011) NOD-like receptors and the innate immune system: coping with danger, damage and death. Cytokine Growth Factor Rev 22: 257-276.
    • (2011) Cytokine Growth Factor Rev , vol.22 , pp. 257-276
    • Kersse, K.1    Bertrand, M.J.2    Lamkanfi, M.3    Vandenabeele, P.4
  • 6
    • 48549102504 scopus 로고    scopus 로고
    • NOD-like receptors (NLRs): bona fide intracellular microbial sensors
    • Shaw MH, Reimer T, Kim YG, Nunez G, (2008) NOD-like receptors (NLRs): bona fide intracellular microbial sensors. Current opinion in immunology 20: 377-382.
    • (2008) Current Opinion in Immunology , vol.20 , pp. 377-382
    • Shaw, M.H.1    Reimer, T.2    Kim, Y.G.3    Nunez, G.4
  • 9
    • 80655144737 scopus 로고    scopus 로고
    • Crystal structure of NALP3 protein pyrin domain (PYD) and its implications in inflammasome assembly
    • Bae JY, Park HH, (2011) Crystal structure of NALP3 protein pyrin domain (PYD) and its implications in inflammasome assembly. The Journal of biological chemistry 286: 39528-39536.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 39528-39536
    • Bae, J.Y.1    Park, H.H.2
  • 10
    • 77956254738 scopus 로고    scopus 로고
    • Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin-pyrin-mediated effector domain signaling in innate immunity
    • Pinheiro AS, Proell M, Eibl C, Page R, Schwarzenbacher R, et al. (2010) Three-dimensional structure of the NLRP7 pyrin domain: insight into pyrin-pyrin-mediated effector domain signaling in innate immunity. The Journal of biological chemistry 285: 27402-27410.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 27402-27410
    • Pinheiro, A.S.1    Proell, M.2    Eibl, C.3    Page, R.4    Schwarzenbacher, R.5
  • 11
    • 33845966052 scopus 로고    scopus 로고
    • Structure and dynamics of ASC2, a pyrin domain-only protein that regulates inflammatory signaling
    • Natarajan A, Ghose R, Hill JM, (2006) Structure and dynamics of ASC2, a pyrin domain-only protein that regulates inflammatory signaling. The Journal of biological chemistry 281: 31863-31875.
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 31863-31875
    • Natarajan, A.1    Ghose, R.2    Hill, J.M.3
  • 12
    • 0042386425 scopus 로고    scopus 로고
    • The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition
    • Liepinsh E, Barbals R, Dahl E, Sharipo A, Staub E, et al. (2003) The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition. Journal of molecular biology 332: 1155-1163.
    • (2003) Journal of Molecular Biology , vol.332 , pp. 1155-1163
    • Liepinsh, E.1    Barbals, R.2    Dahl, E.3    Sharipo, A.4    Staub, E.5
  • 13
    • 0141817846 scopus 로고    scopus 로고
    • NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain
    • Hiller S, Kohl A, Fiorito F, Herrmann T, Wider G, et al. (2003) NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain. Structure 11: 1199-1205.
    • (2003) Structure , vol.11 , pp. 1199-1205
    • Hiller, S.1    Kohl, A.2    Fiorito, F.3    Herrmann, T.4    Wider, G.5
  • 14
    • 77954721051 scopus 로고    scopus 로고
    • Anti-inflammatory activity of PYNOD and its mechanism in humans and mice
    • Imamura R, Wang Y, Kinoshita T, Suzuki M, Noda T, et al. (2010) Anti-inflammatory activity of PYNOD and its mechanism in humans and mice. Journal of immunology 184: 5874-5884.
    • (2010) Journal of Immunology , vol.184 , pp. 5874-5884
    • Imamura, R.1    Wang, Y.2    Kinoshita, T.3    Suzuki, M.4    Noda, T.5
  • 16
    • 84860233490 scopus 로고    scopus 로고
    • NLRP10 is a NOD-like receptor essential to initiate adaptive immunity by dendritic cells
    • Eisenbarth SC, Williams A, Colegio OR, Meng H, Strowig T, et al. (2012) NLRP10 is a NOD-like receptor essential to initiate adaptive immunity by dendritic cells. Nature 484: 510-513.
    • (2012) Nature , vol.484 , pp. 510-513
    • Eisenbarth, S.C.1    Williams, A.2    Colegio, O.R.3    Meng, H.4    Strowig, T.5
  • 18
    • 0033564278 scopus 로고    scopus 로고
    • A robotics-based automated assay for inorganic and organic phosphates
    • Cogan EB, Birrell GB, Griffith OH, (1999) A robotics-based automated assay for inorganic and organic phosphates. Analytical biochemistry 271: 29-35.
    • (1999) Analytical Biochemistry , vol.271 , pp. 29-35
    • Cogan, E.B.1    Birrell, G.B.2    Griffith, O.H.3
  • 19
    • 0032110340 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy
    • Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, et al. (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. Journal of biomolecular NMR 12: 1-23.
    • (1998) Journal of Biomolecular NMR , vol.12 , pp. 1-23
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5
  • 20
    • 0033057676 scopus 로고    scopus 로고
    • A doublet-separated sensitivity-enhanced HSQC for the determination of scalar and dipolar one-bond J-couplings
    • Florence Cordier AJD, Stephan Grzesiek, (1999) A doublet-separated sensitivity-enhanced HSQC for the determination of scalar and dipolar one-bond J-couplings. Journal of Biomolecular NMR 13: 175-180.
    • (1999) Journal of Biomolecular NMR , vol.13 , pp. 175-180
    • Florence Cordier, A.J.D.1    Stephan, G.2
  • 22
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR Structure Determination with Automated NOE Assignment Using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA
    • Herrmann T, Güntert P, Wüthrich K, (2002) Protein NMR Structure Determination with Automated NOE Assignment Using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA. Journal of Molecular Biology 319: 209-227.
    • (2002) Journal of Molecular Biology , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 23
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Gabriel Cornilescu FD, Ad Bax, (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. Journal of Biomolecular NMR 13: 289-302.
    • (1999) Journal of Biomolecular NMR , vol.13 , pp. 289-302
    • Gabriel Cornilescu, F.D.1    Ad, B.2
  • 24
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19
    • Kozakov D, Hall DR, Beglov D, Brenke R, Comeau SR, et al. (2010) Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19. Proteins 78: 3124-3130.
    • (2010) Proteins , vol.78 , pp. 3124-3130
    • Kozakov, D.1    Hall, D.R.2    Beglov, D.3    Brenke, R.4    Comeau, S.R.5
  • 25
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 26
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski RARJ, MacArthur MW, Kaptein R, Thornton JM, (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477-486.
    • (1996) J Biomol NMR , vol.8 , pp. 477-486
    • Laskowski R.A, R.J.1    MacArthur, M.W.2    Kaptein, R.3    Thornton, J.M.4
  • 27
    • 70450250064 scopus 로고    scopus 로고
    • Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC)
    • de Alba E, (2009) Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC). The Journal of biological chemistry 284: 32932-32941.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 32932-32941
    • de Alba, E.1
  • 28
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenstrom P, (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: W545-549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 30
    • 84871314266 scopus 로고    scopus 로고
    • Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein
    • Vajjhala PR, Mirams RE, Hill JM, (2012) Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein. The Journal of biological chemistry 287: 41732-41743.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 41732-41743
    • Vajjhala, P.R.1    Mirams, R.E.2    Hill, J.M.3
  • 32
    • 22544477068 scopus 로고    scopus 로고
    • Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition
    • Chang CI, Ihara K, Chelliah Y, Mengin-Lecreulx D, Wakatsuki S, et al. (2005) Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition. Proc Natl Acad Sci U S A 102: 10279-10284.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10279-10284
    • Chang, C.I.1    Ihara, K.2    Chelliah, Y.3    Mengin-Lecreulx, D.4    Wakatsuki, S.5
  • 33
    • 33645236166 scopus 로고    scopus 로고
    • Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor
    • Chang CI, Chelliah Y, Borek D, Mengin-Lecreulx D, Deisenhofer J, (2006) Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor. Science 311: 1761-1764.
    • (2006) Science , vol.311 , pp. 1761-1764
    • Chang, C.I.1    Chelliah, Y.2    Borek, D.3    Mengin-Lecreulx, D.4    Deisenhofer, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.