메뉴 건너뛰기




Volumn 277, Issue 19, 2010, Pages 3986-3998

Intermodule cooperativity in the structure and dynamics of consecutive complement control modules in human C1r: Structural biology

Author keywords

cooperativity; dynamics; flexibility; modularity; NMR spectroscopy

Indexed keywords

COMPLEMENT COMPONENT C1R; PROTEIN; PROTEIN CCP1; PROTEIN CCP2; UNCLASSIFIED DRUG; C1RL PROTEIN, HUMAN; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN; SERINE PROTEINASE; SOLUTION AND SOLUBILITY;

EID: 77956632484     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07790.x     Document Type: Article
Times cited : (5)

References (63)
  • 1
    • 70349437186 scopus 로고    scopus 로고
    • Complement regulators and inhibitory proteins
    • Zipfel PF Skerka C (2009) Complement regulators and inhibitory proteins. Nat Rev Immunol 9, 729 740.
    • (2009) Nat Rev Immunol , vol.9 , pp. 729-740
    • Zipfel, P.F.1    Skerka, C.2
  • 2
    • 0035849176 scopus 로고    scopus 로고
    • Complement. First of two parts
    • Walport MJ (2001) Complement. First of two parts. N Engl J Med 344, 1140 1144.
    • (2001) N Engl J Med , vol.344 , pp. 1140-1144
    • Walport, M.J.1
  • 3
    • 0035810399 scopus 로고    scopus 로고
    • Complement. Second of two parts
    • Walport MJ (2001) Complement. Second of two parts. N Engl J Med 344, 1058 1066.
    • (2001) N Engl J Med , vol.344 , pp. 1058-1066
    • Walport, M.J.1
  • 4
    • 0024342275 scopus 로고
    • Expression of hemolytically active human complement component C1r proenzyme in insect cells using a baculovirus vector
    • Gál P, Sárvári M, Szilágyi K, Závodszky P Schumaker VN (1989) Expression of hemolytically active human complement component C1r proenzyme in insect cells using a baculovirus vector. Complement Inflamm 6, 433 441.
    • (1989) Complement Inflamm , vol.6 , pp. 433-441
    • Gál, P.1    Sárvári, M.2    Szilágyi, K.3    Závodszky, P.4    Schumaker, V.N.5
  • 5
    • 0023114358 scopus 로고
    • Complete amino acid sequence of the A chain of human complement- classical-pathway enzyme C1r
    • Arlaud GJ, Willis AC Gagnon J (1987) Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r. Biochem J 241, 711 720.
    • (1987) Biochem J , vol.241 , pp. 711-720
    • Arlaud, G.J.1    Willis, A.C.2    Gagnon, J.3
  • 6
    • 0020582458 scopus 로고
    • Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r
    • Arlaud GJ Gagnon J (1983) Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r. Biochemistry 22, 1758 1764.
    • (1983) Biochemistry , vol.22 , pp. 1758-1764
    • Arlaud, G.J.1    Gagnon, J.2
  • 8
    • 0024039803 scopus 로고
    • The role of beta-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX
    • Rees DJG, Jones IM, Handford PA, Walter SJ, Esnouf MP, Smith KJ Brownlee GG (1988) The role of beta-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX. EMBO J 7, 2053 2061.
    • (1988) EMBO J , vol.7 , pp. 2053-2061
    • Rees, D.J.G.1    Jones, I.M.2    Handford, P.A.3    Walter, S.J.4    Esnouf, M.P.5    Smith, K.J.6    Brownlee, G.G.7
  • 10
  • 11
    • 0027190974 scopus 로고
    • The CUB domain. A widespread module in developmentally regulated proteins
    • Bork P Beckmann G (1993) The CUB domain. A widespread module in developmentally regulated proteins. J Mol Biol 231, 539 545.
    • (1993) J Mol Biol , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 12
    • 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, Rossi V, Lunardi T, Thielens NM, Gaboriaud C Arlaud GJ (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, 19340 19348.
    • (2009) J Biol Chem , vol.284 , pp. 19340-19348
    • Bally, I.1    Rossi, V.2    Lunardi, T.3    Thielens, N.M.4    Gaboriaud, C.5    Arlaud, G.J.6
  • 14
    • 0023646322 scopus 로고
    • Detecting homology of distantly related proteins with consensus sequences
    • Patthy L (1987) Detecting homology of distantly related proteins with consensus sequences. FEBS Lett 214, 1 7.
    • (1987) FEBS Lett , vol.214 , pp. 1-7
    • Patthy, L.1
  • 15
    • 0024561914 scopus 로고
    • Structure-function relationships of the complement components
    • Reid KB Day AJ (1989) Structure-function relationships of the complement components. Immunol Today 10, 177 180.
    • (1989) Immunol Today , vol.10 , pp. 177-180
    • Reid, K.B.1    Day, A.J.2
  • 16
    • 0031660179 scopus 로고    scopus 로고
    • Demonstration of a tandem pair of complement protein modules in GABA(B) receptor 1a
    • Hawrot E, Xiao Y, Shi QL, Norman D, Kirkitadze M Barlow PN (1998) Demonstration of a tandem pair of complement protein modules in GABA(B) receptor 1a. FEBS Lett 432, 103 108.
    • (1998) FEBS Lett , vol.432 , pp. 103-108
    • Hawrot, E.1    Xiao, Y.2    Shi, Q.L.3    Norman, D.4    Kirkitadze, M.5    Barlow, P.N.6
  • 20
    • 0033923016 scopus 로고    scopus 로고
    • Functional domains, structural variations and pathogen interactions of MCP, DAF and CR1
    • Hourcade D, Liszewski MK, Krych-Goldberg M Atkinson JP (2000) Functional domains, structural variations and pathogen interactions of MCP, DAF and CR1. Immunopharmacology 49, 103 116.
    • (2000) Immunopharmacology , vol.49 , pp. 103-116
    • Hourcade, D.1    Liszewski, M.K.2    Krych-Goldberg, M.3    Atkinson, J.P.4
  • 21
    • 0035018479 scopus 로고    scopus 로고
    • Structure-function relationships of complement receptor type 1
    • Krych-Goldberg M Atkinson JP (2001) Structure-function relationships of complement receptor type 1. Immunol Rev 180, 112 122.
    • (2001) Immunol Rev , vol.180 , pp. 112-122
    • Krych-Goldberg, M.1    Atkinson, J.P.2
  • 22
    • 0035008505 scopus 로고    scopus 로고
    • Structure and flexibility of the multiple domain proteins that regulate complement activation
    • Kirkitadze MD Barlow PN (2001) Structure and flexibility of the multiple domain proteins that regulate complement activation. Immunol Rev 180, 146 161.
    • (2001) Immunol Rev , vol.180 , pp. 146-161
    • Kirkitadze, M.D.1    Barlow, P.N.2
  • 23
    • 33644537627 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus complement control protein (KCP) binds to heparin and cell surfaces via positively charged amino acids in CCP1-2
    • Mark L, Lee WH, Spiller OB, Villoutreix BO Blom AM (2006) The Kaposi's sarcoma-associated herpesvirus complement control protein (KCP) binds to heparin and cell surfaces via positively charged amino acids in CCP1-2. Mol Immunol 43, 1665 1675.
    • (2006) Mol Immunol , vol.43 , pp. 1665-1675
    • Mark, L.1    Lee, W.H.2    Spiller, O.B.3    Villoutreix, B.O.4    Blom, A.M.5
  • 25
    • 36849044745 scopus 로고    scopus 로고
    • Translational mini-review series on complement factor H: Structural and functional correlations for factor H
    • Schmidt CQ, Herbert AP, Hocking HG, Uhrín D Barlow PN (2008) Translational mini-review series on complement factor H: structural and functional correlations for factor H. Clin Exp Immunol 151, 14 24.
    • (2008) Clin Exp Immunol , vol.151 , pp. 14-24
    • Schmidt, C.Q.1    Herbert, A.P.2    Hocking, H.G.3    Uhrín, D.4    Barlow, P.N.5
  • 26
    • 0030870312 scopus 로고    scopus 로고
    • NMR studies of a viral protein that mimics the regulators of complement activation
    • Wiles AP, Shaw G, Bright J, Perczel A, Campbell ID Barlow PN (1997) NMR studies of a viral protein that mimics the regulators of complement activation. J Mol Biol 272, 253 265.
    • (1997) J Mol Biol , vol.272 , pp. 253-265
    • Wiles, A.P.1    Shaw, G.2    Bright, J.3    Perczel, A.4    Campbell, I.D.5    Barlow, P.N.6
  • 30
    • 33645650398 scopus 로고    scopus 로고
    • Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor
    • Jenkins HT, Mark L, Ball G, Persson J, Lindahl G, Uhrin D, Blom AM Barlow PN (2006) Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor. J Biol Chem 281, 3690 3697.
    • (2006) J Biol Chem , vol.281 , pp. 3690-3697
    • Jenkins, H.T.1    Mark, L.2    Ball, G.3    Persson, J.4    Lindahl, G.5    Uhrin, D.6    Blom, A.M.7    Barlow, P.N.8
  • 31
    • 0034671180 scopus 로고    scopus 로고
    • Identification of the phospholipid-binding site of human beta(2)-glycoprotein i domain v by heteronuclear magnetic resonance
    • Hoshino M, Hagihara Y, Nishii I, Yamazaki T, Kato H Goto Y (2000) Identification of the phospholipid-binding site of human beta(2)-glycoprotein I domain V by heteronuclear magnetic resonance. J Mol Biol 304, 927 939.
    • (2000) J Mol Biol , vol.304 , pp. 927-939
    • Hoshino, M.1    Hagihara, Y.2    Nishii, I.3    Yamazaki, T.4    Kato, H.5    Goto, Y.6
  • 32
    • 33745202838 scopus 로고    scopus 로고
    • Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure
    • Herbert AP, Uhrín D, Lyon M, Pangburn MK Barlow PN (2006) Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure. J Biol Chem 281, 16512 16520.
    • (2006) J Biol Chem , vol.281 , pp. 16512-16520
    • Herbert, A.P.1    Uhrín, D.2    Lyon, M.3    Pangburn, M.K.4    Barlow, P.N.5
  • 33
    • 0035896016 scopus 로고    scopus 로고
    • Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein
    • Henderson CE, Bromek K, Mullin NP, Smith BO, Uhrín D Barlow PN (2001) Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein. J Mol Biol 307, 323 339.
    • (2001) J Mol Biol , vol.307 , pp. 323-339
    • Henderson, C.E.1    Bromek, K.2    Mullin, N.P.3    Smith, B.O.4    Uhrín, D.5    Barlow, P.N.6
  • 34
    • 9144256725 scopus 로고    scopus 로고
    • Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: Only one of the two CCP modules is compactly folded
    • Blein S, Ginham R, Uhrin D, Smith BO, Soares DC, Veltel S, McIlhinney RA, White JH Barlow PN (2004) Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded. J Biol Chem 279, 48292 48306.
    • (2004) J Biol Chem , vol.279 , pp. 48292-48306
    • Blein, S.1    Ginham, R.2    Uhrin, D.3    Smith, B.O.4    Soares, D.C.5    Veltel, S.6    McIlhinney, R.A.7    White, J.H.8    Barlow, P.N.9
  • 35
    • 77951216899 scopus 로고    scopus 로고
    • Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r
    • Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P Gál P (2010) Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r. J Biol Chem 285, 11863 11869.
    • (2010) J Biol Chem , vol.285 , pp. 11863-11869
    • Major, B.1    Kardos, J.2    Kékesi, K.A.3    Lorincz, Z.4    Závodszky, P.5    Gál, P.6
  • 36
  • 37
    • 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, Lacroix M, Thielens NM, Arlaud GJ, Fontecilla-Camps JC Gaboriaud C (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, 231 239.
    • (2002) EMBO J , vol.21 , pp. 231-239
    • Budayova-Spano, M.1    Lacroix, M.2    Thielens, N.M.3    Arlaud, G.J.4    Fontecilla-Camps, J.C.5    Gaboriaud, C.6
  • 38
    • 12144288333 scopus 로고    scopus 로고
    • Same fold with different mobility: Backbone dynamics of small protease inhibitors from the desert locust, Schistocerca gregaria
    • Szenthe B, Gáspári Z, Nagy A, Perczel A Gráf L (2004) Same fold with different mobility: backbone dynamics of small protease inhibitors from the desert locust, Schistocerca gregaria. Biochemistry 43, 3376 3384.
    • (2004) Biochemistry , vol.43 , pp. 3376-3384
    • Szenthe, B.1    Gáspári, Z.2    Nagy, A.3    Perczel, A.4    Gráf, L.5
  • 39
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins
    • Mulder FA, Schipper D, Bott R Boelens R (1999) Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins. J Mol Biol 292, 111 123.
    • (1999) J Mol Biol , vol.292 , pp. 111-123
    • Mulder, F.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4
  • 40
    • 0029872895 scopus 로고    scopus 로고
    • Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions
    • Lefevre JF, Dayie KT, Peng JW Wagner G (1996) Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions. Biochemistry 35, 2674 2686.
    • (1996) Biochemistry , vol.35 , pp. 2674-2686
    • Lefevre, J.F.1    Dayie, K.T.2    Peng, J.W.3    Wagner, G.4
  • 41
    • 10744221921 scopus 로고    scopus 로고
    • Temperature-dependent spectral density analysis applied to monitoring backbone dynamics of major urinary protein-I complexed with the pheromone 2- sec-butyl-4,5-dihydrothiazole
    • Krízová H, Zídek L, Stone MJ, Novotny MV Sklenár V (2004) Temperature-dependent spectral density analysis applied to monitoring backbone dynamics of major urinary protein-I complexed with the pheromone 2- sec-butyl-4,5-dihydrothiazole. J Biomol NMR 28, 369 384.
    • (2004) J Biomol NMR , vol.28 , pp. 369-384
    • Krízová, H.1    Zídek, L.2    Stone, M.J.3    Novotny, M.V.4    Sklenár, V.5
  • 42
    • 2342614819 scopus 로고    scopus 로고
    • Peptide models XLII. Ab initio study on conformational changes of N-formyl-L-histidinamide caused by protonation or deprotonation of its side chain
    • Hudáky P Perczel A (2004) Peptide models XLII. Ab initio study on conformational changes of N-formyl-L-histidinamide caused by protonation or deprotonation of its side chain. J Mol Struct (THEOCHEM) 675, 117 127.
    • (2004) J Mol Struct (THEOCHEM) , vol.675 , pp. 117-127
    • Hudáky, P.1    Perczel, A.2
  • 43
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr DD, Nussinov R Wright PE (2009) The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol 5, 789 796.
    • (2009) Nat Chem Biol , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 44
    • 0025784015 scopus 로고
    • Domain structure and domain-domain interactions of recombinant tissue plasminogen activator
    • Novokhatny VV, Ingham KC Medved LV (1991) Domain structure and domain-domain interactions of recombinant tissue plasminogen activator. J Biol Chem 266, 12994 13002.
    • (1991) J Biol Chem , vol.266 , pp. 12994-13002
    • Novokhatny, V.V.1    Ingham, K.C.2    Medved, L.V.3
  • 50
    • 0022870658 scopus 로고
    • Molecular characterization of the catalytic domains of human complement serine protease C1r
    • Arlaud GJ, Gagnon J, Villiers CL Colomb MG (1986) Molecular characterization of the catalytic domains of human complement serine protease C1r. Biochemistry 25, 5177 5182.
    • (1986) Biochemistry , vol.25 , pp. 5177-5182
    • Arlaud, G.J.1    Gagnon, J.2    Villiers, C.L.3    Colomb, M.G.4
  • 51
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182, 319 326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 53
    • 0004040543 scopus 로고    scopus 로고
    • University of California. San Francisco.
    • Goddard TD Kneller DG (2009) SPARKY 3. University of California, San Francisco.
    • (2009) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 54
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C, Xia T-H, Billeter M, Güntert P Wüthrich K (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomolecular NMR 6, 1 10.
    • (1995) J Biomolecular NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 55
    • 0030207171 scopus 로고    scopus 로고
    • An optimized 3D NOESY-HSQC
    • Talluri S Wagner G (1996) An optimized 3D NOESY-HSQC. J Magn Reson B 112, 200 205.
    • (1996) J Magn Reson B , vol.112 , pp. 200-205
    • Talluri, S.1    Wagner, G.2
  • 57
    • 9444245493 scopus 로고
    • Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek S Bax A (1992) Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114, 6291 6293.
    • (1992) J Am Chem Soc , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 58
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity
    • Muhandiram DR Kay LE (1994) Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity. J Magn Reson B 103, 203 216.
    • (1994) J Magn Reson B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 59
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • Mori S, Abeygunawardana C, Johnson MO van Zijl PC (1995) Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J Magn Reson B 108, 94 98.
    • (1995) J Magn Reson B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    Van Zijl, P.C.4
  • 60
  • 61
    • 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, 719 730.
    • (2000) Biophys J , vol.78 , pp. 719-730
    • García De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 63
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset P, Hus JC, Blackledge M Marion D (2000) Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J Biomol NMR 16, 23 28.
    • (2000) J Biomol NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.C.2    Blackledge, M.3    Marion, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.