메뉴 건너뛰기




Volumn 114, Issue 5, 2017, Pages 986-991

Structure and activation of C1, the complex initiating the classical pathway of the complement cascade

Author keywords

Complement; Innate immunity; Proteolytic cascade; Structural biology

Indexed keywords

COMPLEMENT COMPONENT C1; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M; SERINE PROTEINASE; TETRAMER; RECOMBINANT PROTEIN; SYNTHETIC DNA;

EID: 85011003042     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1616998114     Document Type: Article
Times cited : (76)

References (38)
  • 1
    • 84949497174 scopus 로고    scopus 로고
    • Complement activation, regulation, and molecular basis for complement-related diseases
    • Bajic G, Degn SE, Thiel S, Andersen GR (2015) Complement activation, regulation, and molecular basis for complement-related diseases. EMBO J 34(22):2735-2757.
    • (2015) EMBO J , vol.34 , Issue.22 , pp. 2735-2757
    • Bajic, G.1    Degn, S.E.2    Thiel, S.3    Andersen, G.R.4
  • 2
    • 84919433309 scopus 로고    scopus 로고
    • Deciphering the fine details of c1 assembly and activation mechanisms: "Mission impossible"?
    • Gaboriaud C, Ling WL, Thielens NM, Bally I, Rossi V (2014) Deciphering the fine details of c1 assembly and activation mechanisms: "Mission impossible"? Front Immunol 5:565.
    • (2014) Front Immunol , vol.5 , pp. 565
    • Gaboriaud, C.1    Ling, W.L.2    Thielens, N.M.3    Bally, I.4    Rossi, V.5
  • 3
    • 84882786824 scopus 로고    scopus 로고
    • Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation
    • Venkatraman Girija U, et al. (2013) Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation. Proc Natl Acad Sci USA 110(34):13916-13920.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.34 , pp. 13916-13920
    • Venkatraman Girija, U.1
  • 4
    • 0022395838 scopus 로고
    • Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices
    • Kilchherr E, Hofmann H, Steigemann W, Engel J (1985) Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices. J Mol Biol 186(2):403-415.
    • (1985) J Mol Biol , vol.186 , Issue.2 , pp. 403-415
    • Kilchherr, E.1    Hofmann, H.2    Steigemann, W.3    Engel, J.4
  • 5
    • 77957789299 scopus 로고    scopus 로고
    • Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex
    • Brier S, et al. (2010) Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex. J Biol Chem 285(42):32251-32263.
    • (2010) J Biol Chem , vol.285 , Issue.42 , pp. 32251-32263
    • Brier, S.1
  • 6
    • 84878163798 scopus 로고    scopus 로고
    • Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites
    • Bally I, et al. (2013) Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites. Proc Natl Acad Sci USA 110(21):8650-8655.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.21 , pp. 8650-8655
    • Bally, I.1
  • 7
    • 67749116467 scopus 로고    scopus 로고
    • Identification of the C1q-binding Sites of Human C1r and C1s: A refined three-dimensional model of the C1 complex of complement
    • Bally I, et al. (2009) Identification of the C1q-binding Sites of Human C1r and C1s: A refined three-dimensional model of the C1 complex of complement. J Biol Chem 284(29):19340-19348.
    • (2009) J Biol Chem , vol.284 , Issue.29 , pp. 19340-19348
    • Bally, I.1
  • 9
    • 0036469280 scopus 로고    scopus 로고
    • The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex
    • Budayova-Spano M, et al. (2002) The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex. EMBO J 21(3):231-239.
    • (2002) EMBO J , vol.21 , Issue.3 , pp. 231-239
    • Budayova-Spano, M.1
  • 10
    • 38949188247 scopus 로고    scopus 로고
    • Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r
    • Kardos J, et al. (2008) Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r. Mol Immunol 45(6):1752-1760.
    • (2008) Mol Immunol , vol.45 , Issue.6 , pp. 1752-1760
    • Kardos, J.1
  • 11
    • 84907215709 scopus 로고    scopus 로고
    • Complement activation by ligand-driven juxtaposition of discrete pattern recognition complexes
    • Degn SE, et al. (2014) Complement activation by ligand-driven juxtaposition of discrete pattern recognition complexes. Proc Natl Acad Sci USA 111(37):13445-13450.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.37 , pp. 13445-13450
    • Degn, S.E.1
  • 12
    • 84930188804 scopus 로고    scopus 로고
    • Structural insights into the initiating complex of the lectin pathway of complement activation
    • Kjaer TR, et al. (2015) Structural insights into the initiating complex of the lectin pathway of complement activation. Structure 23(2):342-351.
    • (2015) Structure , vol.23 , Issue.2 , pp. 342-351
    • Kjaer, T.R.1
  • 13
    • 0023114647 scopus 로고
    • Kinetics of C1 activation by a monoclonal anti-C1q antibody and its (Fab)2 fragments
    • Kilchherr E, Schumaker VN, Bianchino AC, Curtiss LK (1987) Kinetics of C1 activation by a monoclonal anti-C1q antibody and its (Fab)2 fragments. J Immunol 138(3):849-855.
    • (1987) J Immunol , vol.138 , Issue.3 , pp. 849-855
    • Kilchherr, E.1    Schumaker, V.N.2    Bianchino, A.C.3    Curtiss, L.K.4
  • 14
    • 0030743802 scopus 로고    scopus 로고
    • Complement recruitment using bispecific diabodies
    • Kontermann RE, Wing MG, Winter G (1997) Complement recruitment using bispecific diabodies. Nat Biotechnol 15(7):629-631.
    • (1997) Nat Biotechnol , vol.15 , Issue.7 , pp. 629-631
    • Kontermann, R.E.1    Wing, M.G.2    Winter, G.3
  • 16
    • 77954312095 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of classical complement activation
    • Kojouharova M, Reid K, Gadjeva M (2010) New insights into the molecular mechanisms of classical complement activation. Mol Immunol 47(13):2154-2160.
    • (2010) Mol Immunol , vol.47 , Issue.13 , pp. 2154-2160
    • Kojouharova, M.1    Reid, K.2    Gadjeva, M.3
  • 17
    • 0018114706 scopus 로고
    • Activation of the first component of human complement (C1) by antibody-antigen aggregates
    • Dodds AW, Sim RB, Porter RR, Kerr MA (1978) Activation of the first component of human complement (C1) by antibody-antigen aggregates. Biochem J 175(2):383-390.
    • (1978) Biochem J , vol.175 , Issue.2 , pp. 383-390
    • Dodds, A.W.1    Sim, R.B.2    Porter, R.R.3    Kerr, M.A.4
  • 18
    • 0028104075 scopus 로고
    • Activation of human complement serine-proteinase C1r is down-regulated by a Ca(2+)-dependent intramolecular control that is released in the C1 complex through a signal transmitted by C1q
    • Thielens NM, Illy C, Bally IM, Arlaud GJ (1994) Activation of human complement serine-proteinase C1r is down-regulated by a Ca(2+)-dependent intramolecular control that is released in the C1 complex through a signal transmitted by C1q. Biochem J 301(Pt 2):509-516.
    • (1994) Biochem J , vol.301 , pp. 509-516
    • Thielens, N.M.1    Illy, C.2    Bally, I.M.3    Arlaud, G.J.4
  • 19
    • 84896055730 scopus 로고    scopus 로고
    • Complement is activated by IgG hexamers assembled at the cell surface
    • Diebolder CA, et al. (2014) Complement is activated by IgG hexamers assembled at the cell surface. Science 343(6176):1260-1263.
    • (2014) Science , vol.343 , Issue.6176 , pp. 1260-1263
    • Diebolder, C.A.1
  • 20
    • 0019168166 scopus 로고
    • Activation of a complex of C1r and C1s subcomponents of human complement C1 by the third subcomponent C1q
    • Lin TY, Fletcher DS (1980) Activation of a complex of C1r and C1s subcomponents of human complement C1 by the third subcomponent C1q. J Biol Chem 255(16):7756-7762.
    • (1980) J Biol Chem , vol.255 , Issue.16 , pp. 7756-7762
    • Lin, T.Y.1    Fletcher, D.S.2
  • 21
    • 0020066129 scopus 로고
    • Spontaneous activation of the first component of human complement (C1) by an intramolecular autocatalytic mechanism
    • Ziccardi RJ (1982) Spontaneous activation of the first component of human complement (C1) by an intramolecular autocatalytic mechanism. J Immunol 128(6):2500-2504.
    • (1982) J Immunol , vol.128 , Issue.6 , pp. 2500-2504
    • Ziccardi, R.J.1
  • 22
    • 0020029096 scopus 로고
    • Kinetics of activation of the first component of complement (C1) by IgG oligomers
    • Tschopp J (1982) Kinetics of activation of the first component of complement (C1) by IgG oligomers. Mol Immunol 19(5):651-657.
    • (1982) Mol Immunol , vol.19 , Issue.5 , pp. 651-657
    • Tschopp, J.1
  • 23
    • 0023201147 scopus 로고
    • Activation of human C1: Analysis with Western blotting reveals slow self-activation
    • Hosoi S, Circolo A, Borsos T (1987) Activation of human C1: Analysis with Western blotting reveals slow self-activation. J Immunol 139(5):1602-1608.
    • (1987) J Immunol , vol.139 , Issue.5 , pp. 1602-1608
    • Hosoi, S.1    Circolo, A.2    Borsos, T.3
  • 24
    • 0024162027 scopus 로고
    • A mechanism for the spontaneous activation of the first component of complement, C1, and its regulation by C1-inhibitor
    • Bianchino AC, Poon PH, Schumaker VN (1988) A mechanism for the spontaneous activation of the first component of complement, C1, and its regulation by C1-inhibitor. J Immunol 141(11):3930-3936.
    • (1988) J Immunol , vol.141 , Issue.11 , pp. 3930-3936
    • Bianchino, A.C.1    Poon, P.H.2    Schumaker, V.N.3
  • 25
    • 0025992308 scopus 로고
    • Spontaneous activation of serum C1 in vitro. Role of C1 inhibitor
    • Tseng Y, Poon PH, Zavodszky P, Schumaker VN (1991) Spontaneous activation of serum C1 in vitro. Role of C1 inhibitor. J Immunol 147(6):1884-1890.
    • (1991) J Immunol , vol.147 , Issue.6 , pp. 1884-1890
    • Tseng, Y.1    Poon, P.H.2    Zavodszky, P.3    Schumaker, V.N.4
  • 26
    • 84983777940 scopus 로고    scopus 로고
    • Antibodies that efficiently form hexamers upon antigen binding can induce complement-dependent cytotoxicity under complement-limiting conditions
    • Cook EM, et al. (2016) Antibodies that efficiently form hexamers upon antigen binding can induce complement-dependent cytotoxicity under complement-limiting conditions. J Immunol 197(5):1762-1775.
    • (2016) J Immunol , vol.197 , Issue.5 , pp. 1762-1775
    • Cook, E.M.1
  • 27
    • 0019472804 scopus 로고
    • Purification and radiolabeling of human C1q
    • Tenner AJ, Lesavre PH, Cooper NR (1981) Purification and radiolabeling of human C1q. J Immunol 127(2):648-653.
    • (1981) J Immunol , vol.127 , Issue.2 , pp. 648-653
    • Tenner, A.J.1    Lesavre, P.H.2    Cooper, N.R.3
  • 28
    • 84934882069 scopus 로고    scopus 로고
    • Automated pipeline for purification, biophysical and X-ray analysis of biomacromolecular solutions
    • Graewert MA, et al. (2015) Automated pipeline for purification, biophysical and X-ray analysis of biomacromolecular solutions. Sci Rep 5:10734.
    • (2015) Sci Rep , vol.5 , pp. 10734
    • Graewert, M.A.1
  • 29
    • 84926366641 scopus 로고    scopus 로고
    • Versatile sample environments and automation for biological solution X-ray scattering experiments at the P12 beamline (PETRA III, DESY)
    • Blanchet CE, et al. (2015) Versatile sample environments and automation for biological solution X-ray scattering experiments at the P12 beamline (PETRA III, DESY). J Appl Cryst 48(Pt 2):431-443.
    • (2015) J Appl Cryst , vol.48 , pp. 431-443
    • Blanchet, C.E.1
  • 30
    • 84863643938 scopus 로고    scopus 로고
    • Automated acquisition and analysis of small angle X-ray scattering data
    • Franke D, Kikhney AG, Svergun DI (2012) Automated acquisition and analysis of small angle X-ray scattering data. Nucl Instrum Methods Phys Res A 689:52-59.
    • (2012) Nucl Instrum Methods Phys Res A , vol.689 , pp. 52-59
    • Franke, D.1    Kikhney, A.G.2    Svergun, D.I.3
  • 31
    • 79953753741 scopus 로고    scopus 로고
    • Improvement of molecular-replacement models with Sculptor
    • Bunkóczi G, Read RJ (2011) Improvement of molecular-replacement models with Sculptor. Acta Crystallogr D Biol Crystallogr 67(Pt 4):303-312.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 303-312
    • Bunkóczi, G.1    Read, R.J.2
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47(Pt 2):110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 33
    • 84982860138 scopus 로고    scopus 로고
    • Solution structures of complement c2 and its C4 complexes propose pathway-specific mechanisms for control and activation of the complement proconvertases
    • Mortensen S, Jensen JK, Andersen GR (2016) Solution structures of complement c2 and its C4 complexes propose pathway-specific mechanisms for control and activation of the complement proconvertases. J Biol Chem 291(32):16494-16507.
    • (2016) J Biol Chem , vol.291 , Issue.32 , pp. 16494-16507
    • Mortensen, S.1    Jensen, J.K.2    Andersen, G.R.3
  • 34
    • 7244253096 scopus 로고    scopus 로고
    • An interactive triple-helical collagen builder
    • Rainey JK, Goh MC (2004) An interactive triple-helical collagen builder. Bioinformatics 20(15):2458-2459.
    • (2004) Bioinformatics , vol.20 , Issue.15 , pp. 2458-2459
    • Rainey, J.K.1    Goh, M.C.2
  • 35
    • 70450106216 scopus 로고    scopus 로고
    • Improved prediction of protein side-chain conformations with SCWRL4
    • Krivov GG, Shapovalov MV, Dunbrack RL, Jr (2009) Improved prediction of protein side-chain conformations with SCWRL4. Proteins 77(4):778-795.
    • (2009) Proteins , vol.77 , Issue.4 , pp. 778-795
    • Krivov, G.G.1    Shapovalov, M.V.2    Dunbrack, R.L.3
  • 36
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • Petoukhov MV, et al. (2012) New developments in the ATSAS program package for small-angle scattering data analysis. J Appl Cryst 45(Pt 2):342-350.
    • (2012) J Appl Cryst , vol.45 , pp. 342-350
    • Petoukhov, M.V.1
  • 37
    • 78649650270 scopus 로고    scopus 로고
    • 3D cryo-EM structure of an active step I spliceosome and localization of its catalytic core
    • Golas MM, et al. (2010) 3D cryo-EM structure of an active step I spliceosome and localization of its catalytic core. Mol Cell 40(6):927-938.
    • (2010) Mol Cell , vol.40 , Issue.6 , pp. 927-938
    • Golas, M.M.1
  • 38
    • 0038016841 scopus 로고    scopus 로고
    • Automatic CTF correction for single particles based upon multivariate statistical analysis of individual power spectra
    • Sander B, Golas MM, Stark H (2003) Automatic CTF correction for single particles based upon multivariate statistical analysis of individual power spectra. J Struct Biol 142(3):392-401.
    • (2003) J Struct Biol , vol.142 , Issue.3 , pp. 392-401
    • Sander, B.1    Golas, M.M.2    Stark, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.