메뉴 건너뛰기




Volumn 51, Issue 37, 2012, Pages 7330-7341

Structural and functional analysis of the NLRP4 pyrin domain

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEINS; BINDING PARTNERS; CHARGED SURFACES; CO-IMMUNOPRECIPITATIONS; CONNECTING LOOPS; CYTOSOLIC RECEPTORS; DEATH DOMAIN; HYDROPHOBIC CORE; INFLAMMATORY RESPONSE; LEUCINE-RICH REPEAT RECEPTORS; NUCLEAR MAGNETIC RESONANCE CHEMICAL SHIFTS; PYRIN DOMAINS; SIGNALING CASCADES; YEAST TWO HYBRID;

EID: 84866386287     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3007059     Document Type: Article
Times cited : (45)

References (65)
  • 1
    • 82955249021 scopus 로고    scopus 로고
    • NOD-like receptors and the innate immune system: Coping with danger, damage and death
    • Kersse, K., Bertrand, M. J., Lamkanfi, M., and 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
  • 2
    • 22444433175 scopus 로고    scopus 로고
    • NLRs join TLRs as innate sensors of pathogens
    • Martinon, F. and Tschopp, J. (2005) NLRs join TLRs as innate sensors of pathogens Trends Immunol. 26, 447-454
    • (2005) Trends Immunol. , vol.26 , pp. 447-454
    • Martinon, F.1    Tschopp, J.2
  • 4
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-β
    • Martinon, F., Burns, K., and Tschopp, J. (2002) The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-β Mol. Cell 10, 417-426
    • (2002) Mol. Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 5
    • 36849045915 scopus 로고    scopus 로고
    • The inflammasome: A danger sensing complex triggering innate immunity
    • Petrilli, V., Dostert, C., Muruve, D. A., and Tschopp, J. (2007) The inflammasome: A danger sensing complex triggering innate immunity Curr. Opin. Immunol. 19, 615-622
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 615-622
    • Petrilli, V.1    Dostert, C.2    Muruve, D.A.3    Tschopp, J.4
  • 7
    • 33845501864 scopus 로고    scopus 로고
    • Apoptosome: A platform for the activation of initiator caspases
    • Bao, Q. and Shi, Y. (2007) Apoptosome: A platform for the activation of initiator caspases Cell Death Differ. 14, 56-65
    • (2007) Cell Death Differ. , vol.14 , pp. 56-65
    • Bao, Q.1    Shi, Y.2
  • 8
  • 9
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A., and Kolodner, R. D. (2001) Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome Nat. Genet. 29, 301-305
    • (2001) Nat. Genet. , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 12
    • 84862815491 scopus 로고    scopus 로고
    • NLRP4 negatively regulates type i interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4
    • Cui, J., Li, Y., Zhu, L., Liu, D., Songyang, Z., Wang, H. Y., and Wang, R. F. (2012) NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4 Nat. Immunol. 13, 387-395
    • (2012) Nat. Immunol. , vol.13 , pp. 387-395
    • Cui, J.1    Li, Y.2    Zhu, L.3    Liu, D.4    Songyang, Z.5    Wang, H.Y.6    Wang, R.F.7
  • 13
    • 0037144586 scopus 로고    scopus 로고
    • A novel PAAD-containing protein that modulates NF-B induction by cytokines tumor necrosis factor-α and interleukin-1β
    • Fiorentino, L., Stehlik, C., Oliveira, V., Ariza, M. E., Godzik, A., and Reed, J. C. (2002) A novel PAAD-containing protein that modulates NF-B induction by cytokines tumor necrosis factor-α and interleukin-1β J. Biol. Chem. 277, 35333-35340
    • (2002) J. Biol. Chem. , vol.277 , pp. 35333-35340
    • Fiorentino, L.1    Stehlik, C.2    Oliveira, V.3    Ariza, M.E.4    Godzik, A.5    Reed, J.C.6
  • 14
    • 50249187691 scopus 로고    scopus 로고
    • Expression analysis of the NLRP gene family suggests a role in human preimplantation development
    • Zhang, P., Dixon, M., Zucchelli, M., Hambiliki, F., Levkov, L., Hovatta, O., and Kere, J. (2008) Expression analysis of the NLRP gene family suggests a role in human preimplantation development PLoS One 3, e2755
    • (2008) PLoS One , vol.3 , pp. 2755
    • Zhang, P.1    Dixon, M.2    Zucchelli, M.3    Hambiliki, F.4    Levkov, L.5    Hovatta, O.6    Kere, J.7
  • 15
    • 79251588741 scopus 로고    scopus 로고
    • NLRP4 negatively regulates autophagic processes through an association with beclin1
    • Jounai, N., Kobiyama, K., Shiina, M., Ogata, K., Ishii, K. J., and Takeshita, F. (2011) NLRP4 negatively regulates autophagic processes through an association with beclin1 J. Immunol. 186, 1646-1655
    • (2011) J. Immunol. , vol.186 , pp. 1646-1655
    • Jounai, N.1    Kobiyama, K.2    Shiina, M.3    Ogata, K.4    Ishii, K.J.5    Takeshita, F.6
  • 16
    • 80655144737 scopus 로고    scopus 로고
    • Crystal structure of NALP3 PYD domain and its implications in inflammasome assembly
    • Bae, J. Y. and Park, H. H. (2011) Crystal structure of NALP3 PYD domain and its implications in inflammasome assembly J. Biol. Chem. 286, 39528-39536
    • (2011) J. Biol. Chem. , vol.286 , pp. 39528-39536
    • Bae, J.Y.1    Park, H.H.2
  • 18
    • 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., and Otting, G. (2003) The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition J. Mol. Biol. 332, 1155-1163
    • (2003) J. Mol. Biol. , vol.332 , pp. 1155-1163
    • Liepinsh, E.1    Barbals, R.2    Dahl, E.3    Sharipo, A.4    Staub, E.5    Otting, G.6
  • 20
    • 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, A. S., Proell, M., Eibl, C., Page, R., Schwarzenbacher, R., and Peti, W. (2010) Three-dimensional structure of the NLRP7 pyrin domain: Insight into pyrin-pyrin-mediated effector domain signaling in innate immunity J. Biol. Chem. 285, 27402-27410
    • (2010) J. Biol. Chem. , vol.285 , pp. 27402-27410
    • Pinheiro, A.S.1    Proell, M.2    Eibl, C.3    Page, R.4    Schwarzenbacher, R.5    Peti, W.6
  • 23
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G. M. (2008) A short history of SHELX Acta Crystallogr. A64, 112-122
    • (2008) Acta Crystallogr. , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 24
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification Acta Crystallogr. D66, 479-485
    • (2010) Acta Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 25
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 27
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. (1988) Multiple sequence alignment with hierarchical clustering Nucleic Acids Res. 16, 10881-10890
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 28
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. and Rosenstrom, P. (2010) Dali server: Conservation mapping in 3D Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 29
    • 40749148575 scopus 로고    scopus 로고
    • On distance and similarity in fold space
    • Sippl, M. J. (2008) On distance and similarity in fold space Bioinformatics 24, 872-873
    • (2008) Bioinformatics , vol.24 , pp. 872-873
    • Sippl, M.J.1
  • 30
    • 38849092210 scopus 로고    scopus 로고
    • A note on difficult structure alignment problems
    • Sippl, M. J. and 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
  • 31
    • 84859379149 scopus 로고    scopus 로고
    • Detection of spatial correlations in protein structures and molecular complexes
    • Sippl, M. J. and Wiederstein, M. (2012) Detection of spatial correlations in protein structures and molecular complexes Structure 20, 718-728
    • (2012) Structure , vol.20 , pp. 718-728
    • Sippl, M.J.1    Wiederstein, M.2
  • 32
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: A protein-protein interaction analysis server
    • Reynolds, C., Damerell, D., and Jones, S. (2009) ProtorP: A protein-protein interaction analysis server Bioinformatics 25, 413-414
    • (2009) Bioinformatics , vol.25 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 33
    • 79955574923 scopus 로고    scopus 로고
    • version 1.2r3pre () Schrödinger, LLC, New York
    • The PyMOL Molecular Graphics System, version 1.2r3pre (2010) Schrödinger, LLC, New York.
    • (2010) The PyMOL Molecular Graphics System
  • 36
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz, R. D. and Woods, R. A. (2002) Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method Methods Enzymol. 350, 87-96
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 37
    • 64249098607 scopus 로고    scopus 로고
    • Evaluation of Nod-like receptor (NLR) effector domain interactions
    • Wagner, R. N., Proell, M., Kufer, T. A., and Schwarzenbacher, R. (2009) Evaluation of Nod-like receptor (NLR) effector domain interactions PLoS One 4, e4931
    • (2009) PLoS One , vol.4 , pp. 4931
    • Wagner, R.N.1    Proell, M.2    Kufer, T.A.3    Schwarzenbacher, R.4
  • 38
    • 33845966052 scopus 로고    scopus 로고
    • Structure and dynamics of ASC2, a pyrin domain-only protein that regulates inflammatory signaling
    • Natarajan, A., Ghose, R., and Hill, J. M. (2006) Structure and dynamics of ASC2, a pyrin domain-only protein that regulates inflammatory signaling J. Biol. Chem. 281, 31863-31875
    • (2006) J. Biol. Chem. , vol.281 , pp. 31863-31875
    • Natarajan, A.1    Ghose, R.2    Hill, J.M.3
  • 40
    • 0038682430 scopus 로고    scopus 로고
    • The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-B and pro-caspase-1 regulation
    • Stehlik, C., Krajewska, M., Welsh, K., Krajewski, S., Godzik, A., and Reed, J. C. (2003) The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-B and pro-caspase-1 regulation Biochem. J. 373, 101-113
    • (2003) Biochem. J. , vol.373 , pp. 101-113
    • Stehlik, C.1    Krajewska, M.2    Welsh, K.3    Krajewski, S.4    Godzik, A.5    Reed, J.C.6
  • 41
    • 0035425256 scopus 로고    scopus 로고
    • The death domain superfamily: A tale of two interfaces?
    • Weber, C. H. and Vincenz, C. (2001) The death domain superfamily: A tale of two interfaces? Trends Biochem. Sci. 26, 475-481
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 43
    • 33751423867 scopus 로고    scopus 로고
    • Solution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RIC
    • Manon, F., Favier, A., Nunez, G., Simorre, J. P., and Cusack, S. (2007) Solution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RIC J. Mol. Biol. 365, 160-174
    • (2007) J. Mol. Biol. , vol.365 , pp. 160-174
    • Manon, F.1    Favier, A.2    Nunez, G.3    Simorre, J.P.4    Cusack, S.5
  • 44
    • 33846036718 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary crystallographic characterization of the caspase-recruitment domain of human Nod1
    • Srimathi, T., Robbins, S. L., Dubas, R. L., Seo, J. H., and Park, Y. C. (2007) Purification, crystallization and preliminary crystallographic characterization of the caspase-recruitment domain of human Nod1 Acta Crystallogr. F63, 21-23
    • (2007) Acta Crystallogr. , vol.63 , pp. 21-23
    • Srimathi, T.1    Robbins, S.L.2    Dubas, R.L.3    Seo, J.H.4    Park, Y.C.5
  • 48
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-β and related growth factors: Implications for site-directed mutagenesis
    • Innis, C. A., Shi, J., and Blundell, T. L. (2000) Evolutionary trace analysis of TGF-β and related growth factors: Implications for site-directed mutagenesis Protein Eng. 13, 839-847
    • (2000) Protein Eng. , vol.13 , pp. 839-847
    • Innis, C.A.1    Shi, J.2    Blundell, T.L.3
  • 49
    • 0042512008 scopus 로고    scopus 로고
    • Homology modeling provides insights into the binding mode of the PAAD/DAPIN/pyrin domain, a fourth member of the CARD/DD/DED domain family
    • Liu, T., Rojas, A., Ye, Y., and Godzik, A. (2003) Homology modeling provides insights into the binding mode of the PAAD/DAPIN/pyrin domain, a fourth member of the CARD/DD/DED domain family Protein Sci. 12, 1872-1881
    • (2003) Protein Sci. , vol.12 , pp. 1872-1881
    • Liu, T.1    Rojas, A.2    Ye, Y.3    Godzik, A.4
  • 51
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • Park, H. H., Logette, E., Raunser, S., Cuenin, S., Walz, T., Tschopp, J., and Wu, H. (2007) Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex Cell 128, 533-546
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1    Logette, E.2    Raunser, S.3    Cuenin, S.4    Walz, T.5    Tschopp, J.6    Wu, H.7
  • 53
    • 0033613210 scopus 로고    scopus 로고
    • Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: A structural basis for specific adaptor/caspase interaction
    • Zhou, P., Chou, J., Olea, R. S., Yuan, J., and Wagner, G. (1999) Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: A structural basis for specific adaptor/caspase interaction Proc. Natl. Acad. Sci. U.S.A. 96, 11265-11270
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11265-11270
    • Zhou, P.1    Chou, J.2    Olea, R.S.3    Yuan, J.4    Wagner, G.5
  • 55
    • 0035916324 scopus 로고    scopus 로고
    • The pyrin domain: A possible member of the death domain-fold family implicated in apoptosis and inflammation
    • Martinon, F., Hofmann, K., and Tschopp, J. (2001) The pyrin domain: A possible member of the death domain-fold family implicated in apoptosis and inflammation Curr. Biol. 11, R118-R120
    • (2001) Curr. Biol. , vol.11
    • Martinon, F.1    Hofmann, K.2    Tschopp, J.3
  • 56
    • 3142674847 scopus 로고    scopus 로고
    • Heterotypic interactions among NACHT domains: Implications for regulation of innate immune responses
    • Damiano, J. S., Oliveira, V., Welsh, K., and Reed, J. C. (2004) Heterotypic interactions among NACHT domains: Implications for regulation of innate immune responses Biochem. J. 381, 213-219
    • (2004) Biochem. J. , vol.381 , pp. 213-219
    • Damiano, J.S.1    Oliveira, V.2    Welsh, K.3    Reed, J.C.4
  • 57
    • 77649176543 scopus 로고    scopus 로고
    • Overcoming the solubility limit with solubility-enhancement tags: Successful applications in biomolecular NMR studies
    • Zhou, P. and Wagner, G. (2010) Overcoming the solubility limit with solubility-enhancement tags: Successful applications in biomolecular NMR studies J. Biomol. NMR 46, 23-31
    • (2010) J. Biomol. NMR , vol.46 , pp. 23-31
    • Zhou, P.1    Wagner, G.2
  • 58
    • 69549086803 scopus 로고    scopus 로고
    • Evolution and functional divergence of NLRP genes in mammalian reproductive systems
    • Tian, X., Pascal, G., and Monget, P. (2009) Evolution and functional divergence of NLRP genes in mammalian reproductive systems BMC Evol. Biol. 9, 202
    • (2009) BMC Evol. Biol. , vol.9 , pp. 202
    • Tian, X.1    Pascal, G.2    Monget, P.3
  • 59
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1
    • Qin, H., Srinivasula, S. M., Wu, G., Fernandes-Alnemri, T., Alnemri, E. S., and Shi, Y. (1999) Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1 Nature 399, 549-557
    • (1999) Nature , vol.399 , pp. 549-557
    • Qin, H.1    Srinivasula, S.M.2    Wu, G.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5    Shi, Y.6
  • 60
    • 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) J. Biol. Chem. 284, 32932-32941
    • (2009) J. Biol. Chem. , vol.284 , pp. 32932-32941
    • De Alba, E.1
  • 61
    • 77957794023 scopus 로고    scopus 로고
    • Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus
    • Esposito, D., Sankar, A., Morgner, N., Robinson, C. V., Rittinger, K., and Driscoll, P. C. (2010) Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus Structure 18, 1378-1390
    • (2010) Structure , vol.18 , pp. 1378-1390
    • Esposito, D.1    Sankar, A.2    Morgner, N.3    Robinson, C.V.4    Rittinger, K.5    Driscoll, P.C.6
  • 62
    • 79952189807 scopus 로고    scopus 로고
    • Structural analyses of death domains and their interactions
    • Park, H. H. (2011) Structural analyses of death domains and their interactions Apoptosis 16, 209-220
    • (2011) Apoptosis , vol.16 , pp. 209-220
    • Park, H.H.1
  • 63
    • 0035066836 scopus 로고    scopus 로고
    • Global indicators of X-ray data quality
    • Weiss, M. S. (2001) Global indicators of X-ray data quality J. Appl. Crystallogr. 34, 130-135
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 130-135
    • Weiss, M.S.1
  • 64
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 65
    • 0032031476 scopus 로고    scopus 로고
    • Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of γb- and βb2-crystallin
    • Tickle, I. J., Laskowski, R. A., and Moss, D. S. (1998) Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of γB- and βB2-crystallin Acta Crystallogr. D54, 243-252
    • (1998) Acta Crystallogr. , vol.54 , pp. 243-252
    • Tickle, I.J.1    Laskowski, R.A.2    Moss, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.