메뉴 건너뛰기




Volumn 110, Issue 34, 2013, Pages 13916-13920

Correction: Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation (Proceedings of the National Academy of Sciences of the United States of America (2013) 110 (13916-13920) DOI: 10.1073/pnas.1311113110);Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation

Author keywords

Innate immunity; Structural biology

Indexed keywords

CALCIUM; COLLAGEN; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE; COMPLEMENT COMPONENT C1; PROTEIN BINDING;

EID: 84882786824     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1615704113     Document Type: Erratum
Times cited : (83)

References (32)
  • 1
    • 77955883153 scopus 로고    scopus 로고
    • Complement: A key system for immune surveillance and homeostasis
    • Ricklin D, Hajishengallis G, Yang K, Lambris JD (2010) Complement: A key system for immune surveillance and homeostasis. Nat Immunol 11(9):785-797.
    • (2010) Nat Immunol , vol.11 , Issue.9 , pp. 785-797
    • Ricklin, D.1    Hajishengallis, G.2    Yang, K.3    Lambris, J.D.4
  • 2
    • 70350041296 scopus 로고    scopus 로고
    • Paths reunited: Initiation of the classical and lectin pathways of complement activation
    • Wallis R, Mitchell DA, Schmid R, Schwaeble WJ, Keeble AH (2010) Paths reunited: Initiation of the classical and lectin pathways of complement activation. Immunobiology 215(1):1-11.
    • (2010) Immunobiology , vol.215 , Issue.1 , pp. 1-11
    • Wallis, R.1    Mitchell, D.A.2    Schmid, R.3    Schwaeble, W.J.4    Keeble, A.H.5
  • 3
    • 84862628488 scopus 로고    scopus 로고
    • The modular serine proteases of the complement cascade
    • Forneris F, Wu J, Gros P (2012) The modular serine proteases of the complement cascade. Curr Opin Struct Biol 22(3):333-341.
    • (2012) Curr Opin Struct Biol , vol.22 , Issue.3 , pp. 333-341
    • Forneris, F.1    Wu, J.2    Gros, P.3
  • 4
    • 0019168322 scopus 로고
    • Assembly of subcomponents C1r and C1s of first component of complement: Electron microscopic and ultracentrifugal studies
    • Tschopp J, Villiger W, Fuchs H, Kilchherr E, Engel J (1980) Assembly of subcomponents C1r and C1s of first component of complement: Electron microscopic and ultracentrifugal studies. Proc Natl Acad Sci USA 77(12):7014-7018.
    • (1980) Proc Natl Acad Sci USA , vol.77 , Issue.12 , pp. 7014-7018
    • Tschopp, J.1    Villiger, W.2    Fuchs, H.3    Kilchherr, E.4    Engel, J.5
  • 5
    • 0041856103 scopus 로고    scopus 로고
    • X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement
    • Gregory LA, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C (2003) X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement. J Biol Chem 278(34):32157-32164.
    • (2003) J Biol Chem , vol.278 , Issue.34 , pp. 32157-32164
    • Gregory, L.A.1    Thielens, N.M.2    Arlaud, G.J.3    Fontecilla-Camps, J.C.4    Gaboriaud, C.5
  • 6
    • 0037904914 scopus 로고    scopus 로고
    • Crystal structure of the CUB1-EGF-CUB2 region of mannosebinding protein associated serine protease-2
    • Feinberg H, et al. (2003) Crystal structure of the CUB1-EGF-CUB2 region of mannosebinding protein associated serine protease-2. EMBO J 22(10):2348-2359.
    • (2003) EMBO J , vol.22 , Issue.10 , pp. 2348-2359
    • Feinberg, H.1
  • 7
    • 54449087793 scopus 로고    scopus 로고
    • Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins
    • Teillet F, et al. (2008) Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins. J Biol Chem 283(37):25715-25724.
    • (2008) J Biol Chem , vol.283 , Issue.37 , pp. 25715-25724
    • Teillet, F.1
  • 8
    • 0021794049 scopus 로고
    • Molecular modelling of human complement subcomponent C1q and its complex with C1r2C1s2 derived from neutron-scattering curves and hydrodynamic properties
    • Perkins SJ (1985) Molecular modelling of human complement subcomponent C1q and its complex with C1r2C1s2 derived from neutron-scattering curves and hydrodynamic properties. Biochem J 228(1):13-26.
    • (1985) Biochem J , vol.228 , Issue.1 , pp. 13-26
    • Perkins, S.J.1
  • 9
    • 0020033478 scopus 로고
    • Ultrastructure of the first component of human complement: Electron microscopy of the crosslinked complex
    • Strang CJ, Siegel RC, Phillips ML, Poon PH, Schumaker VN (1982) Ultrastructure of the first component of human complement: Electron microscopy of the crosslinked complex. Proc Natl Acad Sci USA 79(2):586-590.
    • (1982) Proc Natl Acad Sci USA , vol.79 , Issue.2 , pp. 586-590
    • Strang, C.J.1    Siegel, R.C.2    Phillips, M.L.3    Poon, P.H.4    Schumaker, V.N.5
  • 10
    • 0019139892 scopus 로고
    • Calcium binding properties of the C1 subcomponents C1q, C1r and C1s
    • Villiers CL, Arlaud GJ, Painter RH, Colomb MG (1980) Calcium binding properties of the C1 subcomponents C1q, C1r and C1s. FEBS Lett 117(1):289-294.
    • (1980) FEBS Lett , vol.117 , Issue.1 , pp. 289-294
    • Villiers, C.L.1    Arlaud, G.J.2    Painter, R.H.3    Colomb, M.G.4
  • 11
    • 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
  • 12
    • 67649232598 scopus 로고    scopus 로고
    • Analogous interactions in initiating complexes of the classical and lectin pathways of complement
    • Phillips AE, et al. (2009) Analogous interactions in initiating complexes of the classical and lectin pathways of complement. J Immunol 182(12):7708-7717.
    • (2009) J Immunol , vol.182 , Issue.12 , pp. 7708-7717
    • Phillips, A.E.1
  • 13
    • 0018423264 scopus 로고
    • Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement
    • Reid KB (1979) Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement. Biochem J 179(2):367-371.
    • (1979) Biochem J , vol.179 , Issue.2 , pp. 367-371
    • Reid, K.B.1
  • 14
    • 1842740356 scopus 로고    scopus 로고
    • Localization of the serine protease-binding sites in the collagenlike domain of mannose-binding protein: Indirect effects of naturally occurring mutations on protease binding and activation
    • Wallis R, et al. (2004) Localization of the serine protease-binding sites in the collagenlike domain of mannose-binding protein: Indirect effects of naturally occurring mutations on protease binding and activation. J Biol Chem 279(14):14065-14073.
    • (2004) J Biol Chem , vol.279 , Issue.14 , pp. 14065-14073
    • Wallis, R.1
  • 15
    • 80855128787 scopus 로고    scopus 로고
    • Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: Implications for complement activation
    • Gingras AR, et al. (2011) Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: Implications for complement activation. Structure 19(11):1635-1643.
    • (2011) Structure , vol.19 , Issue.11 , pp. 1635-1643
    • Gingras, A.R.1
  • 16
    • 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
  • 17
    • 84863775185 scopus 로고    scopus 로고
    • A molecular dynamics study of C1r and C1s dimers: Implications for the structure of the C1 complex
    • Beveridge AJ, Wallis R, Samani NJ (2012) A molecular dynamics study of C1r and C1s dimers: Implications for the structure of the C1 complex. Proteins 80(8):1987-1997.
    • (2012) Proteins , vol.80 , Issue.8 , pp. 1987-1997
    • Beveridge, A.J.1    Wallis, R.2    Samani, N.J.3
  • 18
    • 84878407764 scopus 로고    scopus 로고
    • A molecular switch governs the interaction between human complement protease C1s and its substrate, complement C4
    • Perry AJ, et al. (2013) A molecular switch governs the interaction between human complement protease C1s and its substrate, complement C4. J Biol Chem 288(22): 15821-15829.
    • (2013) J Biol Chem , vol.288 , Issue.22 , pp. 15821-15829
    • Perry, A.J.1
  • 19
    • 0034678903 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human complement c1s: A serine protease with a handle
    • Gaboriaud C, Rossi V, Bally I, Arlaud GJ, Fontecilla-Camps JC (2000) Crystal structure of the catalytic domain of human complement c1s: A serine protease with a handle. EMBO J 19(8):1755-1765.
    • (2000) EMBO J , vol.19 , Issue.8 , pp. 1755-1765
    • Gaboriaud, C.1    Rossi, V.2    Bally, I.3    Arlaud, G.J.4    Fontecilla-Camps, J.C.5
  • 20
    • 0017663985 scopus 로고
    • Purification of proenzymic and activated human C1s free ofC1r. Effect of calcium and ionic strength on activated C1s
    • Arlaud GJ, Reboul A, Meyer CM, Colomb MG (1977) Purification of proenzymic and activated human C1s free ofC1r. Effect of calcium and ionic strength on activated C1s. Biochim Biophys Acta 485(1):215-225.
    • (1977) Biochim Biophys Acta , vol.485 , Issue.1 , pp. 215-225
    • Arlaud, G.J.1    Reboul, A.2    Meyer, C.M.3    Colomb, M.G.4
  • 21
    • 0017073905 scopus 로고
    • Circular-dichroism and electronmicroscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin
    • Brodsky-Doyle B, Leonard KR, Reid KB (1976) Circular-dichroism and electronmicroscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin. Biochem J 159(2):279-286.
    • (1976) Biochem J , vol.159 , Issue.2 , pp. 279-286
    • Brodsky-Doyle, B.1    Leonard, K.R.2    Reid, K.B.3
  • 22
    • 0025953624 scopus 로고
    • Measurement of macromolecular interactions between complement subcomponents C1q, C1r, C1s, and immunoglobulin IgM by sedimentation analysis using the analytical ultracentrifuge
    • Poon PH, Schumaker VN (1991) Measurement of macromolecular interactions between complement subcomponents C1q, C1r, C1s, and immunoglobulin IgM by sedimentation analysis using the analytical ultracentrifuge. J Biol Chem 266(9): 5723-5727.
    • (1991) J Biol Chem , vol.266 , Issue.9 , pp. 5723-5727
    • Poon, P.H.1    Schumaker, V.N.2
  • 23
    • 77951216899 scopus 로고    scopus 로고
    • Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r
    • Major B, et al. (2010) Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r. J Biol Chem 285(16): 11863-11869.
    • (2010) J Biol Chem , vol.285 , Issue.16 , pp. 11863-11869
    • Major, B.1
  • 24
    • 84866558185 scopus 로고    scopus 로고
    • Structural basis for activation of the complement system by component C4 cleavage
    • Kidmose RT, et al. (2012) Structural basis for activation of the complement system by component C4 cleavage. Proc Natl Acad Sci USA 109(38):15425-15430.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.38 , pp. 15425-15430
    • Kidmose, R.T.1
  • 25
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , Issue.PART 4 , pp. 658-674
    • McCoy, A.J.1
  • 26
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution
    • Bella J, Eaton M, Brodsky B, Berman HM (1994) Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. Science 266(5182):75-81.
    • (1994) Science , vol.266 , Issue.5182 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 27
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53(Pt 3): 240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 28
    • 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 D Biol Crystallogr 50(Pt 5):760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763
  • 29
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 30
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García De La Torre J, Huertas ML, Carrasco B (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys J 78(2): 719-730.
    • (2000) Biophys J , vol.78 , Issue.2 , pp. 719-730
    • García De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 31
    • 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
  • 32
    • 0344012497 scopus 로고    scopus 로고
    • The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties
    • Gaboriaud C, et al. (2003) The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J Biol Chem 278(47):46974-46982.
    • (2003) J Biol Chem , vol.278 , Issue.47 , pp. 46974-46982
    • Gaboriaud, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.