메뉴 건너뛰기




Volumn 424, Issue 5, 2012, Pages 295-312

Solution structure of CCP modules 10-12 illuminates functional architecture of the complement regulator, factor H

Author keywords

complement system; protein domains; protein NMR; regulators of complement activation; small angle X ray scattering

Indexed keywords

COMPLEMENT; COMPLEMENT CONTROL PROTEIN 10; COMPLEMENT CONTROL PROTEIN 11; COMPLEMENT CONTROL PROTEIN 12; COMPLEMENT CONTROL PROTEIN 13; COMPLEMENT CONTROL PROTEIN 14; COMPLEMENT CONTROL PROTEIN 15; COMPLEMENT FACTOR H; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84869215409     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.09.013     Document Type: Article
Times cited : (24)

References (88)
  • 1
    • 0035810399 scopus 로고    scopus 로고
    • Complement. First of two parts
    • M.J. Walport Complement. First of two parts N. Engl. J. Med. 344 2001 1058 1066
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1058-1066
    • Walport, M.J.1
  • 2
    • 0035849176 scopus 로고    scopus 로고
    • Complement. Second of two parts
    • M.J. Walport Complement. Second of two parts N. Engl. J. Med. 344 2001 1140 1144
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1140-1144
    • Walport, M.J.1
  • 3
    • 77955883153 scopus 로고    scopus 로고
    • Complement: A key system for immune surveillance and homeostasis
    • D. Ricklin, G. Hajishengallis, K. Yang, and J.D. Lambris Complement: a key system for immune surveillance and homeostasis Nat. Immunol. 11 2010 785 797
    • (2010) Nat. Immunol. , vol.11 , pp. 785-797
    • Ricklin, D.1    Hajishengallis, G.2    Yang, K.3    Lambris, J.D.4
  • 4
    • 0019501478 scopus 로고
    • Formation of the initial C3 convertase of the alternative complement pathway. Acquisition of C3b-like activities by spontaneous hydrolysis of the putative thioester in native C3
    • M.K. Pangburn, R.D. Schreiber, and H.J. Muller-Eberhard Formation of the initial C3 convertase of the alternative complement pathway. Acquisition of C3b-like activities by spontaneous hydrolysis of the putative thioester in native C3 J. Exp. Med. 154 1981 856 867
    • (1981) J. Exp. Med. , vol.154 , pp. 856-867
    • Pangburn, M.K.1    Schreiber, R.D.2    Muller-Eberhard, H.J.3
  • 5
    • 77953266787 scopus 로고    scopus 로고
    • The amplification loop of the complement pathways
    • P.J. Lachmann The amplification loop of the complement pathways Adv. Immunol. 104 2009 115 149
    • (2009) Adv. Immunol. , vol.104 , pp. 115-149
    • Lachmann, P.J.1
  • 6
    • 0345176684 scopus 로고
    • Evidence for presence of an internal thiolester bond in third component of human complement
    • B.F. Tack, R.A. Harrison, J. Janatova, M.L. Thomas, and J.W. Prahl Evidence for presence of an internal thiolester bond in third component of human complement Proc. Natl Acad. Sci. USA 77 1980 5764 5768
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 5764-5768
    • Tack, B.F.1    Harrison, R.A.2    Janatova, J.3    Thomas, M.L.4    Prahl, J.W.5
  • 7
    • 0035008505 scopus 로고    scopus 로고
    • Structure and flexibility of the multiple domain proteins that regulate complement activation
    • M.D. Kirkitadze, and P.N. Barlow Structure and flexibility of the multiple domain proteins that regulate complement activation Immunol. Rev. 180 2001 146 161
    • (2001) Immunol. Rev. , vol.180 , pp. 146-161
    • Kirkitadze, M.D.1    Barlow, P.N.2
  • 8
    • 0025314311 scopus 로고
    • Discrimination between activators and nonactivators of the alternative pathway of complement: Regulation via a sialic acid/polyanion binding site on factor H
    • S. Meri, and M.K. Pangburn Discrimination between activators and nonactivators of the alternative pathway of complement: regulation via a sialic acid/polyanion binding site on factor H Proc. Natl Acad. Sci. USA 87 1990 3982 3986
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 3982-3986
    • Meri, S.1    Pangburn, M.K.2
  • 9
    • 0025023338 scopus 로고
    • The leukocyte cell surface receptor(s) for the iC3b product of complement
    • H. Rosen, and S.K. Law The leukocyte cell surface receptor(s) for the iC3b product of complement Curr. Top. Microbiol. Immunol. 153 1990 99 122
    • (1990) Curr. Top. Microbiol. Immunol. , vol.153 , pp. 99-122
    • Rosen, H.1    Law, S.K.2
  • 11
    • 0012042656 scopus 로고
    • Control of the amplification convertase of complement by the plasma protein β1H
    • J.M. Weiler, M.R. Daha, K.F. Austen, and D.T. Fearon Control of the amplification convertase of complement by the plasma protein β1H Proc. Natl Acad. Sci. USA 73 1976 3268 3272
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 3268-3272
    • Weiler, J.M.1    Daha, M.R.2    Austen, K.F.3    Fearon, D.T.4
  • 13
    • 36849084660 scopus 로고    scopus 로고
    • Translational mini-review series on complement factor H: Genetics and disease associations of human complement factor H
    • S.R. de Cordoba, and E.G. de Jorge Translational mini-review series on complement factor H: genetics and disease associations of human complement factor H Clin. Exp. Immunol. 151 2008 1 13
    • (2008) Clin. Exp. Immunol. , vol.151 , pp. 1-13
    • De Cordoba, S.R.1    De Jorge, E.G.2
  • 14
    • 21044453724 scopus 로고    scopus 로고
    • A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration
    • G.S. Hageman, D.H. Anderson, L.V. Johnson, L.S. Hancox, A.J. Taiber, and L.I. Hardisty A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration Proc. Natl Acad. Sci. USA 102 2005 7227 7232
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 7227-7232
    • Hageman, G.S.1    Anderson, D.H.2    Johnson, L.V.3    Hancox, L.S.4    Taiber, A.J.5    Hardisty, L.I.6
  • 15
    • 0033921990 scopus 로고    scopus 로고
    • Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement
    • M.K. Pangburn Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement Immunopharmacology 49 2000 149 157
    • (2000) Immunopharmacology , vol.49 , pp. 149-157
    • Pangburn, M.K.1
  • 16
    • 36849044745 scopus 로고    scopus 로고
    • Translational mini-review series on complement factor H: Structural and functional correlations for factor H
    • C.Q. Schmidt, A.P. Herbert, H.G. Hocking, D. Uhrin, and P.N. Barlow Translational mini-review series on complement factor H: structural and functional correlations for factor H Clin. Exp. Immunol. 151 2008 14 24
    • (2008) Clin. Exp. Immunol. , vol.151 , pp. 14-24
    • Schmidt, C.Q.1    Herbert, A.P.2    Hocking, H.G.3    Uhrin, D.4    Barlow, P.N.5
  • 17
    • 29744453472 scopus 로고    scopus 로고
    • Opportunities for new therapies based on the natural regulators of complement activation
    • E. Brook, A.P. Herbert, H.T. Jenkins, D.C. Soares, and P.N. Barlow Opportunities for new therapies based on the natural regulators of complement activation Ann. N. Y. Acad. Sci. 1056 2005 176 188
    • (2005) Ann. N. Y. Acad. Sci. , vol.1056 , pp. 176-188
    • Brook, E.1    Herbert, A.P.2    Jenkins, H.T.3    Soares, D.C.4    Barlow, P.N.5
  • 19
    • 36048937343 scopus 로고    scopus 로고
    • Complement-targeted therapeutics
    • D. Ricklin, and J.D. Lambris Complement-targeted therapeutics Nat. Biotechnol. 25 2007 1265 1275
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1265-1275
    • Ricklin, D.1    Lambris, J.D.2
  • 20
    • 0024561914 scopus 로고
    • Structure-function relationships of the complement components
    • K.B. Reid, and A.J. Day Structure-function relationships of the complement components Immunol. Today 10 1989 177 180
    • (1989) Immunol. Today , vol.10 , pp. 177-180
    • Reid, K.B.1    Day, A.J.2
  • 21
    • 0022578840 scopus 로고
    • Partial characterization of human complement factor H by protein and cDNA sequencing: Homology with other complement and non-complement proteins
    • J. Ripoche, A.J. Day, A.C. Willis, K.T. Belt, R.D. Campbell, and R.B. Sim Partial characterization of human complement factor H by protein and cDNA sequencing: homology with other complement and non-complement proteins Biosci. Rep. 6 1986 65 72
    • (1986) Biosci. Rep. , vol.6 , pp. 65-72
    • Ripoche, J.1    Day, A.J.2    Willis, A.C.3    Belt, K.T.4    Campbell, R.D.5    Sim, R.B.6
  • 22
    • 0023875503 scopus 로고
    • The complete amino acid sequence of human complement factor H
    • J. Ripoche, A.J. Day, T.J. Harris, and R.B. Sim The complete amino acid sequence of human complement factor H Biochem. J. 249 1988 593 602
    • (1988) Biochem. J. , vol.249 , pp. 593-602
    • Ripoche, J.1    Day, A.J.2    Harris, T.J.3    Sim, R.B.4
  • 23
    • 0025727462 scopus 로고
    • Oligomeric domain structure of human complement factor H by X-ray and neutron solution scattering
    • S.J. Perkins, A.S. Nealis, and R.B. Sim Oligomeric domain structure of human complement factor H by X-ray and neutron solution scattering Biochemistry 30 1991 2847 2857
    • (1991) Biochemistry , vol.30 , pp. 2847-2857
    • Perkins, S.J.1    Nealis, A.S.2    Sim, R.B.3
  • 24
    • 0026645955 scopus 로고
    • Ultrastructures and interactions of complement factors H and i
    • R.G. DiScipio Ultrastructures and interactions of complement factors H and I J. Immunol. 149 1992 2592 2599
    • (1992) J. Immunol. , vol.149 , pp. 2592-2599
    • Discipio, R.G.1
  • 25
    • 0035933335 scopus 로고    scopus 로고
    • Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling
    • M. Aslam, and S.J. Perkins Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling J. Mol. Biol. 309 2001 1117 1138
    • (2001) J. Mol. Biol. , vol.309 , pp. 1117-1138
    • Aslam, M.1    Perkins, S.J.2
  • 26
    • 36349016373 scopus 로고    scopus 로고
    • The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties
    • A.I. Okemefuna, H.E. Gilbert, K.M. Griggs, R.J. Ormsby, D.L. Gordon, and S.J. Perkins The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties J. Mol. Biol. 375 2008 80 101
    • (2008) J. Mol. Biol. , vol.375 , pp. 80-101
    • Okemefuna, A.I.1    Gilbert, H.E.2    Griggs, K.M.3    Ormsby, R.J.4    Gordon, D.L.5    Perkins, S.J.6
  • 28
  • 30
    • 33745202838 scopus 로고    scopus 로고
    • Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in 3D structure
    • A.P. Herbert, D. Uhrin, M. Lyon, M.K. Pangburn, and P.N. Barlow Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in 3D structure J. Biol. Chem. 281 2006 16512 16520
    • (2006) J. Biol. Chem. , vol.281 , pp. 16512-16520
    • Herbert, A.P.1    Uhrin, D.2    Lyon, M.3    Pangburn, M.K.4    Barlow, P.N.5
  • 31
    • 33646164894 scopus 로고    scopus 로고
    • Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome
    • T.S. Jokiranta, V.P. Jaakola, M.J. Lehtinen, M. Parepalo, S. Meri, and A. Goldman Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome EMBO J. 25 2006 1784 1794
    • (2006) EMBO J. , vol.25 , pp. 1784-1794
    • Jokiranta, T.S.1    Jaakola, V.P.2    Lehtinen, M.J.3    Parepalo, M.4    Meri, S.5    Goldman, A.6
  • 33
    • 44049086967 scopus 로고    scopus 로고
    • Structure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variations
    • H.G. Hocking, A.P. Herbert, D. Kavanagh, D.C. Soares, V.P. Ferreira, and M.K. Pangburn Structure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variations J. Biol. Chem. 283 2008 9475 9487
    • (2008) J. Biol. Chem. , vol.283 , pp. 9475-9487
    • Hocking, H.G.1    Herbert, A.P.2    Kavanagh, D.3    Soares, D.C.4    Ferreira, V.P.5    Pangburn, M.K.6
  • 34
    • 67649230210 scopus 로고    scopus 로고
    • Structure of complement fragment C3b-factor H and implications for host protection by complement regulators
    • J. Wu, Y.Q. Wu, D. Ricklin, B.J. Janssen, J.D. Lambris, and P. Gros Structure of complement fragment C3b-factor H and implications for host protection by complement regulators Nat. Immunol. 10 2009 728 733
    • (2009) Nat. Immunol. , vol.10 , pp. 728-733
    • Wu, J.1    Wu, Y.Q.2    Ricklin, D.3    Janssen, B.J.4    Lambris, J.D.5    Gros, P.6
  • 35
    • 70450225410 scopus 로고    scopus 로고
    • The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module
    • C.Q. Schmidt, A.P. Herbert, H.D. Mertens, M. Guariento, D.C. Soares, and D. Uhrin The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module J. Mol. Biol. 395 2010 105 122
    • (2010) J. Mol. Biol. , vol.395 , pp. 105-122
    • Schmidt, C.Q.1    Herbert, A.P.2    Mertens, H.D.3    Guariento, M.4    Soares, D.C.5    Uhrin, D.6
  • 36
    • 84857536091 scopus 로고    scopus 로고
    • Structural analysis of the C-terminal region (modules 18-20) of complement regulator factor H (FH)
    • H.P. Morgan, H.D. Mertens, M. Guariento, C.Q. Schmidt, D.C. Soares, and D.I. Svergun Structural analysis of the C-terminal region (modules 18-20) of complement regulator factor H (FH) PLoS One 7 2012 e32187
    • (2012) PLoS One , vol.7 , pp. 32187
    • Morgan, H.P.1    Mertens, H.D.2    Guariento, M.3    Schmidt, C.Q.4    Soares, D.C.5    Svergun, D.I.6
  • 38
    • 81755172091 scopus 로고    scopus 로고
    • Use of time-resolved FRET to validate crystal structure of complement regulatory complex between C3b and factor H (N terminus)
    • I.C. Pechtl, R.K. Neely, D.T. Dryden, A.C. Jones, and P.N. Barlow Use of time-resolved FRET to validate crystal structure of complement regulatory complex between C3b and factor H (N terminus) Protein Sci. 20 2011 2102 2112
    • (2011) Protein Sci. , vol.20 , pp. 2102-2112
    • Pechtl, I.C.1    Neely, R.K.2    Dryden, D.T.3    Jones, A.C.4    Barlow, P.N.5
  • 39
    • 0021736976 scopus 로고
    • Localization of the complement-component-C3b-binding site and the cofactor activity for factor i in the 38 kDa tryptic fragment of factor H
    • J. Alsenz, J.D. Lambris, T.F. Schulz, and M.P. Dierich Localization of the complement-component-C3b-binding site and the cofactor activity for factor I in the 38 kDa tryptic fragment of factor H Biochem. J. 224 1984 389 398
    • (1984) Biochem. J. , vol.224 , pp. 389-398
    • Alsenz, J.1    Lambris, J.D.2    Schulz, T.F.3    Dierich, M.P.4
  • 41
    • 0029763437 scopus 로고    scopus 로고
    • Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis
    • A.K. Sharma, and M.K. Pangburn Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis Proc. Natl Acad. Sci. USA 93 1996 10996 11001
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10996-11001
    • Sharma, A.K.1    Pangburn, M.K.2
  • 42
    • 0029850245 scopus 로고    scopus 로고
    • Mapping of the domains required for decay acceleration activity of the human factor H-like protein 1 and factor H
    • S. Kuhn, and P.F. Zipfel Mapping of the domains required for decay acceleration activity of the human factor H-like protein 1 and factor H Eur. J. Immunol. 26 1996 2383 2387
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2383-2387
    • Kuhn, S.1    Zipfel, P.F.2
  • 43
    • 0026044042 scopus 로고
    • Localization of the heparin-binding site on complement factor H
    • M.K. Pangburn, M.A. Atkinson, and S. Meri Localization of the heparin-binding site on complement factor H J. Biol. Chem. 266 1991 16847 16853
    • (1991) J. Biol. Chem. , vol.266 , pp. 16847-16853
    • Pangburn, M.K.1    Atkinson, M.A.2    Meri, S.3
  • 45
    • 33750336175 scopus 로고    scopus 로고
    • Critical role of the C-terminal domains of factor H in regulating complement activation at cell surfaces
    • V.P. Ferreira, A.P. Herbert, H.G. Hocking, P.N. Barlow, and M.K. Pangburn Critical role of the C-terminal domains of factor H in regulating complement activation at cell surfaces J. Immunol. 177 2006 6308 6316
    • (2006) J. Immunol. , vol.177 , pp. 6308-6316
    • Ferreira, V.P.1    Herbert, A.P.2    Hocking, H.G.3    Barlow, P.N.4    Pangburn, M.K.5
  • 46
    • 67449119124 scopus 로고    scopus 로고
    • The binding of factor H to a complex of physiological polyanions and C3b on cells is impaired in atypical hemolytic uremic syndrome
    • V.P. Ferreira, A.P. Herbert, C. Cortes, K.A. McKee, B.S. Blaum, and S.T. Esswein The binding of factor H to a complex of physiological polyanions and C3b on cells is impaired in atypical hemolytic uremic syndrome J. Immunol. 182 2009 7009 7018
    • (2009) J. Immunol. , vol.182 , pp. 7009-7018
    • Ferreira, V.P.1    Herbert, A.P.2    Cortes, C.3    McKee, K.A.4    Blaum, B.S.5    Esswein, S.T.6
  • 49
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • P. Guntert Automated NMR structure calculation with CYANA Methods Mol. Biol. 278 2004 353 378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 50
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • A.T. Brunger Version 1.2 of the crystallography and NMR system Nat. Protoc. 2 2007 2728 2733
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 51
    • 3242887525 scopus 로고    scopus 로고
    • STRIDE: A web server for secondary structure assignment from known atomic coordinates of proteins
    • M. Heinig, and D. Frishman STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins Nucleic Acids Res. 32 2004 W500 W502
    • (2004) Nucleic Acids Res. , vol.32
    • Heinig, M.1    Frishman, D.2
  • 52
    • 0037155690 scopus 로고    scopus 로고
    • Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor
    • B.O. Smith, R.L. Mallin, M. Krych-Goldberg, X. Wang, R.E. Hauhart, and K. Bromek Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor Cell 108 2002 769 780
    • (2002) Cell , vol.108 , pp. 769-780
    • Smith, B.O.1    Mallin, R.L.2    Krych-Goldberg, M.3    Wang, X.4    Hauhart, R.E.5    Bromek, K.6
  • 53
    • 78149347784 scopus 로고    scopus 로고
    • Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens
    • B.D. Persson, N.B. Schmitz, C. Santiago, G. Zocher, M. Larvie, and U. Scheu Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens PLoS Pathog. 6 2010 e1001122
    • (2010) PLoS Pathog. , vol.6 , pp. 1001122
    • Persson, B.D.1    Schmitz, N.B.2    Santiago, C.3    Zocher, G.4    Larvie, M.5    Scheu, U.6
  • 54
  • 56
    • 80053025476 scopus 로고    scopus 로고
    • Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings
    • M. Maciejewski, N. Tjandra, and P.N. Barlow Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings Biochemistry 50 2011 8138 8149
    • (2011) Biochemistry , vol.50 , pp. 8138-8149
    • MacIejewski, M.1    Tjandra, N.2    Barlow, P.N.3
  • 57
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • D. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 58
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • D. Franke, and D.I. Svergun DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering J. Appl. Crystallogr. 42 2009 342 346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 59
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • M.B. Kozin, and D.I. Svergun Automated matching of high- and low-resolution structural models J. Appl. Crystallogr. 34 2001 33 41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 60
    • 77956641793 scopus 로고    scopus 로고
    • Solution structure of the 128 kDa enzyme i dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering
    • C.D. Schwieters, J.Y. Suh, A. Grishaev, R. Ghirlando, Y. Takayama, and G.M. Clore Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering J. Am. Chem. Soc. 132 2010 13026 13045
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13026-13045
    • Schwieters, C.D.1    Suh, J.Y.2    Grishaev, A.3    Ghirlando, R.4    Takayama, Y.5    Clore, G.M.6
  • 61
    • 1542317796 scopus 로고    scopus 로고
    • How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?
    • G.M. Clore, and C.D. Schwieters How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation? J. Am. Chem. Soc. 126 2004 2923 2938
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2923-2938
    • Clore, G.M.1    Schwieters, C.D.2
  • 62
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • P. Bernado, E. Mylonas, M.V. Petoukhov, M. Blackledge, and D.I. Svergun Structural characterization of flexible proteins using small-angle X-ray scattering J. Am. Chem. Soc. 129 2007 5656 5664
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 65
    • 67651095769 scopus 로고    scopus 로고
    • Electrostatic interactions contribute to the folded-back conformation of wild type human factor H
    • A.I. Okemefuna, R. Nan, J. Gor, and S.J. Perkins Electrostatic interactions contribute to the folded-back conformation of wild type human factor H J. Mol. Biol. 391 2009 98 118
    • (2009) J. Mol. Biol. , vol.391 , pp. 98-118
    • Okemefuna, A.I.1    Nan, R.2    Gor, J.3    Perkins, S.J.4
  • 66
    • 33847385391 scopus 로고    scopus 로고
    • Combined use of 2,4,6-trihydroxyacetophenone as matrix and enzymatic deglycosylation in organic-aqueous solvent systems for the simultaneous characterization of complex glycoproteins and N-glycans by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • F. Fenaille, M. Le Mignon, C. Groseil, L. Siret, and N. Bihoreau Combined use of 2,4,6-trihydroxyacetophenone as matrix and enzymatic deglycosylation in organic-aqueous solvent systems for the simultaneous characterization of complex glycoproteins and N-glycans by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Rapid Commun. Mass Spectrom. 21 2007 812 816
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 812-816
    • Fenaille, F.1    Le Mignon, M.2    Groseil, C.3    Siret, L.4    Bihoreau, N.5
  • 67
    • 0032832221 scopus 로고    scopus 로고
    • Co-operativity between modules within a C3b-binding site of complement receptor type 1
    • M.D. Kirkitadze, D.T. Dryden, S.M. Kelly, N.C. Price, X. Wang, and M. Krych Co-operativity between modules within a C3b-binding site of complement receptor type 1 FEBS Lett. 459 1999 133 138
    • (1999) FEBS Lett. , vol.459 , pp. 133-138
    • Kirkitadze, M.D.1    Dryden, D.T.2    Kelly, S.M.3    Price, N.C.4    Wang, X.5    Krych, M.6
  • 68
    • 0033153280 scopus 로고    scopus 로고
    • Independently melting modules and highly structured intermodular junctions within complement receptor type 1
    • M.D. Kirkitadze, M. Krych, D. Uhrin, D.T. Dryden, B.O. Smith, and A. Cooper Independently melting modules and highly structured intermodular junctions within complement receptor type 1 Biochemistry 38 1999 7019 7031
    • (1999) Biochemistry , vol.38 , pp. 7019-7031
    • Kirkitadze, M.D.1    Krych, M.2    Uhrin, D.3    Dryden, D.T.4    Smith, B.O.5    Cooper, A.6
  • 69
    • 20344387872 scopus 로고    scopus 로고
    • The structure of interleukin-2 complexed with its alpha receptor
    • M. Rickert, X. Wang, M.J. Boulanger, N. Goriatcheva, and K.C. Garcia The structure of interleukin-2 complexed with its alpha receptor Science 308 2005 1477 1480
    • (2005) Science , vol.308 , pp. 1477-1480
    • Rickert, M.1    Wang, X.2    Boulanger, M.J.3    Goriatcheva, N.4    Garcia, K.C.5
  • 71
    • 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
    • S. Blein, R. Ginham, D. Uhrin, B.O. Smith, D.C. Soares, and S. Veltel 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 2004 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
  • 72
    • 44349192171 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins based on the meta approach
    • T. Ishida, and K. Kinoshita Prediction of disordered regions in proteins based on the meta approach Bioinformatics 24 2008 1344 1348
    • (2008) Bioinformatics , vol.24 , pp. 1344-1348
    • Ishida, T.1    Kinoshita, K.2
  • 73
    • 33645851021 scopus 로고    scopus 로고
    • The C-terminus of complement regulator Factor H mediates target recognition: Evidence for a compact conformation of the native protein
    • M. Oppermann, T. Manuelian, M. Jozsi, E. Brandt, T.S. Jokiranta, and S. Heinen The C-terminus of complement regulator Factor H mediates target recognition: evidence for a compact conformation of the native protein Clin. Exp. Immunol. 144 2006 342 352
    • (2006) Clin. Exp. Immunol. , vol.144 , pp. 342-352
    • Oppermann, M.1    Manuelian, T.2    Jozsi, M.3    Brandt, E.4    Jokiranta, T.S.5    Heinen, S.6
  • 74
    • 79151485902 scopus 로고    scopus 로고
    • Production of biologically active complement factor H in therapeutically useful quantities
    • C.Q. Schmidt, F.C. Slingsby, A. Richards, and P.N. Barlow Production of biologically active complement factor H in therapeutically useful quantities Protein Expression Purif. 76 2011 254 263
    • (2011) Protein Expression Purif. , vol.76 , pp. 254-263
    • Schmidt, C.Q.1    Slingsby, F.C.2    Richards, A.3    Barlow, P.N.4
  • 75
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: Development of a software pipeline
    • W.F. Vranken, W. Boucher, T.J. Stevens, R.H. Fogh, A. Pajon, and M. Llinas The CCPN data model for NMR spectroscopy: development of a software pipeline Proteins 59 2005 687 696
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Stevens, T.J.3    Fogh, R.H.4    Pajon, A.5    Llinas, M.6
  • 79
    • 29744434976 scopus 로고    scopus 로고
    • Complement control protein modules in the regulators of complement activation
    • D. Morikis, J.D. Lambris, CRC Press, Taylor & Francis Group Boca Raton, FL
    • D.C. Soares, and P.N. Barlow Complement control protein modules in the regulators of complement activation D. Morikis, J.D. Lambris, Structural Biology of the Complement System 2005 CRC Press, Taylor & Francis Group Boca Raton, FL 19 62
    • (2005) Structural Biology of the Complement System , pp. 19-62
    • Soares, D.C.1    Barlow, P.N.2
  • 80
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • I.N. Shindyalov, and P.E. Bourne Protein structure alignment by incremental combinatorial extension (CE) of the optimal path Protein Eng. 11 1998 739 747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 83
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux tres petits angles: Application a l'etude de phenomenes ultramicroscopiques
    • A. Guinier La diffraction des rayons X aux tres petits angles: application a l'etude de phenomenes ultramicroscopiques Ann. Phys. (Paris) 12 1939 161 237
    • (1939) Ann. Phys. (Paris) , vol.12 , pp. 161-237
    • Guinier, A.1
  • 84
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 85
    • 33846839463 scopus 로고    scopus 로고
    • A physical picture of atomic motions within the Dickerson DNA dodecamer in solution derived from joint ensemble refinement against NMR and large-angle X-ray scattering data
    • C.D. Schwieters, and G.M. Clore A physical picture of atomic motions within the Dickerson DNA dodecamer in solution derived from joint ensemble refinement against NMR and large-angle X-ray scattering data Biochemistry 46 2007 1152 1166
    • (2007) Biochemistry , vol.46 , pp. 1152-1166
    • Schwieters, C.D.1    Clore, G.M.2
  • 86
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J. Appl. Crystallogr. 36 2003 860 864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 87
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • M.V. Petoukhov, and D.I. Svergun Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.