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Volumn 347, Issue 5, 2005, Pages 965-978

Evidence for structural plasticity of heavy chain complementarity- determining region 3 in antibody-ssDNA recognition

Author keywords

Anti DNA antibodies; DNA binding proteins; Hemihedral twinning; Systemic lupus erythematosus; X ray crystallography

Indexed keywords

DNA ANTIBODY; DNA BASE; IMMUNOGLOBULIN F(AB) FRAGMENT; SINGLE STRANDED DNA; TYROSINE;

EID: 15344351500     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.02.008     Document Type: Article
Times cited : (27)

References (83)
  • 3
    • 0037298948 scopus 로고    scopus 로고
    • Anti-DNA antibodies: Aspects of structure and pathogenicity
    • Y.J. Jang, and B.D. Stollar Anti-DNA antibodies: aspects of structure and pathogenicity Cell. Mol. Life Sci. 60 2003 309 320
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 309-320
    • Jang, Y.J.1    Stollar, B.D.2
  • 4
    • 0025275488 scopus 로고
    • A role for immunogenic DNA in the pathogenesis of systemic lupus erythematosus
    • D.S. Pisetsky, J.P. Grudier, and G.S. Gilkeson A role for immunogenic DNA in the pathogenesis of systemic lupus erythematosus Arthritis Rheum. 33 1990 153 159
    • (1990) Arthritis Rheum. , vol.33 , pp. 153-159
    • Pisetsky, D.S.1    Grudier, J.P.2    Gilkeson, G.S.3
  • 5
    • 0039539926 scopus 로고
    • Avidity of anti-DNA antibodies in serum and IgG glomerular eluates from patients with systemic lupus erythematosus. Associations of high avidity antinative DNA antibody with glomerulonephritis
    • J.B. Winfield, I. Faiferman, and D. Koffler Avidity of anti-DNA antibodies in serum and IgG glomerular eluates from patients with systemic lupus erythematosus. Associations of high avidity antinative DNA antibody with glomerulonephritis J. Clin. Invest. 59 1991 90 95
    • (1991) J. Clin. Invest. , vol.59 , pp. 90-95
    • Winfield, J.B.1    Faiferman, I.2    Koffler, D.3
  • 6
    • 0025868411 scopus 로고
    • Sulfated glycolipids are the platelet autoantigens for human platelet-binding monoclonal anti-DNA autoantibodies
    • H. Murakami, Z. Lam, B.C. Furie, V.N. Reinhold, T. Asano, and B. Furie Sulfated glycolipids are the platelet autoantigens for human platelet-binding monoclonal anti-DNA autoantibodies J. Biol. Chem. 266 1991 15414 15419
    • (1991) J. Biol. Chem. , vol.266 , pp. 15414-15419
    • Murakami, H.1    Lam, Z.2    Furie, B.C.3    Reinhold, V.N.4    Asano, T.5    Furie, B.6
  • 8
    • 0033180545 scopus 로고    scopus 로고
    • Anti-DNA autoantibodies and systemic lupus erythematosus
    • N.B. Blatt, and G.D. Glick Anti-DNA autoantibodies and systemic lupus erythematosus Pharmacol. Ther. 83 1999 125 139
    • (1999) Pharmacol. Ther. , vol.83 , pp. 125-139
    • Blatt, N.B.1    Glick, G.D.2
  • 9
    • 0025116451 scopus 로고
    • The role of anti-DNA antibodies in lupus nephritis
    • M. Waer The role of anti-DNA antibodies in lupus nephritis Clin. Rheumatol. Suppl. 1 9 1990 111 114
    • (1990) Clin. Rheumatol. Suppl. 1 , vol.9 , pp. 111-114
    • Waer, M.1
  • 10
    • 0028069658 scopus 로고
    • The origin, sequence, structure, and consequences of developing anti-DNA antibodies. A human perspective
    • D.A. Isenberg, M.R. Ehrenstein, C. Longhurst, and J.K. Kalsi The origin, sequence, structure, and consequences of developing anti-DNA antibodies. A human perspective Arthritis Rheum. 37 1994 169 180
    • (1994) Arthritis Rheum. , vol.37 , pp. 169-180
    • Isenberg, D.A.1    Ehrenstein, M.R.2    Longhurst, C.3    Kalsi, J.K.4
  • 11
    • 0028096717 scopus 로고
    • Structure-function correlates of autoantibodies to nucleic acids. Lessons from immunochemical, genetic and structural studies
    • D. Eilat, and W.F. Anderson Structure-function correlates of autoantibodies to nucleic acids. Lessons from immunochemical, genetic and structural studies Mol. Immunol. 31 1994 1377 1390
    • (1994) Mol. Immunol. , vol.31 , pp. 1377-1390
    • Eilat, D.1    Anderson, W.F.2
  • 12
    • 12244313937 scopus 로고    scopus 로고
    • Anti-DNA antibodies-structure and function
    • A. Rahman, S. Kumar, and K.N. Potter Anti-DNA antibodies-structure and function Lupus 11 2002 776 779
    • (2002) Lupus , vol.11 , pp. 776-779
    • Rahman, A.1    Kumar, S.2    Potter, K.N.3
  • 13
    • 0029073665 scopus 로고
    • Immunospecific reduction of antioligonucleotide antibody-forming cells with a tetrakis-oligonucleotide conjugate (LJP 394), a therapeutic candidate for the treatment of lupus nephritis
    • D.S. Jones, P.A. Barstad, M.J. Feild, J.P. Hachmann, M.S. Hayag, and K.W. Hill Immunospecific reduction of antioligonucleotide antibody-forming cells with a tetrakis-oligonucleotide conjugate (LJP 394), a therapeutic candidate for the treatment of lupus nephritis J. Med. Chem. 38 1995 2138 2144
    • (1995) J. Med. Chem. , vol.38 , pp. 2138-2144
    • Jones, D.S.1    Barstad, P.A.2    Feild, M.J.3    Hachmann, J.P.4    Hayag, M.S.5    Hill, K.W.6
  • 14
    • 0036949954 scopus 로고    scopus 로고
    • Workshop report on some new ideas about the treatment of systemic lupus erythematosus
    • M. Linnik, N.A. Staines, J. Berden, and D.A. Isenberg Workshop report on some new ideas about the treatment of systemic lupus erythematosus Lupus 11 2002 793 796
    • (2002) Lupus , vol.11 , pp. 793-796
    • Linnik, M.1    Staines, N.A.2    Berden, J.3    Isenberg, D.A.4
  • 15
    • 0023816089 scopus 로고
    • Specific inhibition of the DNA-anti-DNA immune reaction by low molecular weight anionic compounds
    • E. Ben-Chetrit, D. Eilat, and S.A. Ben-Sasson Specific inhibition of the DNA-anti-DNA immune reaction by low molecular weight anionic compounds Immunology 65 1988 479 485
    • (1988) Immunology , vol.65 , pp. 479-485
    • Ben-Chetrit, E.1    Eilat, D.2    Ben-Sasson, S.A.3
  • 16
    • 0033038935 scopus 로고    scopus 로고
    • Molecular mimicry between bacterial and self antigen in a patient with systemic lupus erythematosus
    • C. Kowal, A. Weinstein, and B. Diamond Molecular mimicry between bacterial and self antigen in a patient with systemic lupus erythematosus Eur. J. Immunol. 29 1999 1901 1911
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1901-1911
    • Kowal, C.1    Weinstein, A.2    Diamond, B.3
  • 17
    • 0034953516 scopus 로고    scopus 로고
    • Crossreactivity of human anti-dsDNA antibodies to phosphorylcholine: Clues to their origin
    • A. Sharma, D.A. Isenberg, and B. Diamond Crossreactivity of human anti-dsDNA antibodies to phosphorylcholine: clues to their origin J. Autoimmun. 16 2001 479 484
    • (2001) J. Autoimmun. , vol.16 , pp. 479-484
    • Sharma, A.1    Isenberg, D.A.2    Diamond, B.3
  • 18
    • 0035060979 scopus 로고    scopus 로고
    • Lupus anti-DNA autoantibodies cross-react with a glomerular structural protein: A case for tissue injury by molecular mimicry
    • G. Mostoslavsky, R. Fischel, N. Yachimovich, Y. Yarkoni, E. Rosenmann, and M. Monestier Lupus anti-DNA autoantibodies cross-react with a glomerular structural protein: a case for tissue injury by molecular mimicry Eur. J. Immunol. 31 2001 1221 1227
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1221-1227
    • Mostoslavsky, G.1    Fischel, R.2    Yachimovich, N.3    Yarkoni, Y.4    Rosenmann, E.5    Monestier, M.6
  • 20
    • 0035173156 scopus 로고    scopus 로고
    • A subset of lupus anti-DNA antibodies cross-reacts with the NR2 glutamate receptor in systemic lupus erythematosus
    • L.A. DeGiorgio, K.N. Konstantinov, S.C. Lee, J.A. Hardin, B.T. Volpe, and B. Diamond A subset of lupus anti-DNA antibodies cross-reacts with the NR2 glutamate receptor in systemic lupus erythematosus Nature Med. 7 2001 1189 1193
    • (2001) Nature Med. , vol.7 , pp. 1189-1193
    • Degiorgio, L.A.1    Konstantinov, K.N.2    Lee, S.C.3    Hardin, J.A.4    Volpe, B.T.5    Diamond, B.6
  • 21
    • 0030910657 scopus 로고    scopus 로고
    • Mimotopes of polyreactive anti-DNA antibodies identified using phage-display peptide libraries
    • P. Sibille, T. Ternynck, F. Nato, G. Buttin, D. Strosberg, and A. Avrameas Mimotopes of polyreactive anti-DNA antibodies identified using phage-display peptide libraries Eur. J. Immunol. 27 1997 1221 1228
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1221-1228
    • Sibille, P.1    Ternynck, T.2    Nato, F.3    Buttin, G.4    Strosberg, D.5    Avrameas, A.6
  • 22
    • 0027729268 scopus 로고
    • Isolation and characterization of nucleic acid-binding antibody fragments from autoimmune mice-derived bacteriophage display libraries
    • M.J. Calcutt, M.T. Kremer, M.F. Giblin, T.P. Quinn, and S.L. Deutscher Isolation and characterization of nucleic acid-binding antibody fragments from autoimmune mice-derived bacteriophage display libraries Gene 137 1993 77 83
    • (1993) Gene , vol.137 , pp. 77-83
    • Calcutt, M.J.1    Kremer, M.T.2    Giblin, M.F.3    Quinn, T.P.4    Deutscher, S.L.5
  • 24
    • 0032586844 scopus 로고    scopus 로고
    • Characteristics of the immunoglobulin Vkappa genes, pseudogenes, relics and orphons in the mouse genome
    • K.F. Schable, R. Thiebe, A. Bensch, J. Brensing-Kuppers, V. Heim, and T. Kirschbaum Characteristics of the immunoglobulin Vkappa genes, pseudogenes, relics and orphons in the mouse genome Eur. J. Immunol. 29 1999 2082 2086
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2082-2086
    • Schable, K.F.1    Thiebe, R.2    Bensch, A.3    Brensing-Kuppers, J.4    Heim, V.5    Kirschbaum, T.6
  • 26
    • 0037252714 scopus 로고    scopus 로고
    • IMGT, the international ImMunoGeneTics database
    • M.P. Lefranc IMGT, the international ImMunoGeneTics database Nucl. Acids Res. 31 2003 307 310
    • (2003) Nucl. Acids Res. , vol.31 , pp. 307-310
    • Lefranc, M.P.1
  • 27
    • 0030063744 scopus 로고    scopus 로고
    • Ligand recognition by anti-DNA autoantibodies. Affinity, specificity, and mode of binding
    • P.C. Swanson, C. Ackroyd, and G.D. Glick Ligand recognition by anti-DNA autoantibodies. Affinity, specificity, and mode of binding Biochemistry 35 1996 1624 1633
    • (1996) Biochemistry , vol.35 , pp. 1624-1633
    • Swanson, P.C.1    Ackroyd, C.2    Glick, G.D.3
  • 28
    • 0033547834 scopus 로고    scopus 로고
    • Evidence for sequence-specific recognition of DNA by anti-single-stranded DNA autoantibodies
    • S.Y. Stevens, and G.D. Glick Evidence for sequence-specific recognition of DNA by anti-single-stranded DNA autoantibodies Biochemistry 38 1999 560 568
    • (1999) Biochemistry , vol.38 , pp. 560-568
    • Stevens, S.Y.1    Glick, G.D.2
  • 29
    • 0035814884 scopus 로고    scopus 로고
    • Thermodynamic basis for sequence-specific recognition of ssDNA by an autoantibody
    • P.C. Ackroyd, J. Cleary, and G.D. Glick Thermodynamic basis for sequence-specific recognition of ssDNA by an autoantibody Biochemistry 40 2001 2911 2922
    • (2001) Biochemistry , vol.40 , pp. 2911-2922
    • Ackroyd, P.C.1    Cleary, J.2    Glick, G.D.3
  • 30
    • 0037435584 scopus 로고    scopus 로고
    • Mutational analysis of a sequence-specific ssDNA binding lupus autoantibody
    • J. Cleary, and G.D. Glick Mutational analysis of a sequence-specific ssDNA binding lupus autoantibody Biochemistry 42 2003 30 41
    • (2003) Biochemistry , vol.42 , pp. 30-41
    • Cleary, J.1    Glick, G.D.2
  • 31
    • 0028270037 scopus 로고
    • High resolution epitope mapping of an anti-DNA autoantibody using model DNA ligands
    • P.C. Swanson, B.C. Cooper, and G.D. Glick High resolution epitope mapping of an anti-DNA autoantibody using model DNA ligands J. Immunol. 152 1994 2601 2612
    • (1994) J. Immunol. , vol.152 , pp. 2601-2612
    • Swanson, P.C.1    Cooper, B.C.2    Glick, G.D.3
  • 32
    • 0025939121 scopus 로고
    • An autoantibody to single-stranded DNA: Comparison of the three-dimensional structures of the unliganded Fab and a deoxynucleotide-Fab complex
    • J.N. Herron, X.M. He, D.W. Ballard, P.R. Blier, P.E. Pace, and A.L.M. Bothwell An autoantibody to single-stranded DNA: comparison of the three-dimensional structures of the unliganded Fab and a deoxynucleotide-Fab complex Proteins: Struct. Funct. Genet. 11 1991 159 175
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 159-175
    • Herron, J.N.1    He, X.M.2    Ballard, D.W.3    Blier, P.R.4    Pace, P.E.5    Bothwell, A.L.M.6
  • 33
    • 0030776843 scopus 로고    scopus 로고
    • Site-specific mutagenesis of a recombinant anti-single-stranded DNA Fab. Role of heavy chain complementarity-determining region 3 residues in antigen interaction
    • A.A. Komissarov, M.T. Marchbank, M.J. Calcutt, T.P. Quinn, and S.L. Deutscher Site-specific mutagenesis of a recombinant anti-single-stranded DNA Fab. Role of heavy chain complementarity-determining region 3 residues in antigen interaction J. Biol. Chem. 272 1997 26864 26870
    • (1997) J. Biol. Chem. , vol.272 , pp. 26864-26870
    • Komissarov, A.A.1    Marchbank, M.T.2    Calcutt, M.J.3    Quinn, T.P.4    Deutscher, S.L.5
  • 34
    • 0033517851 scopus 로고    scopus 로고
    • Thermodynamics of Fab/DNA interactions: Contributions of heavy chain complementarity determining region 3
    • A.A. Komissarov, and S.L. Deutscher Thermodynamics of Fab/DNA interactions: contributions of heavy chain complementarity determining region 3 Biochemistry 38 1999 14631 14637
    • (1999) Biochemistry , vol.38 , pp. 14631-14637
    • Komissarov, A.A.1    Deutscher, S.L.2
  • 35
    • 0035824870 scopus 로고    scopus 로고
    • Crystal structure of an antigen-binding fragment bound to single-stranded DNA
    • J.J. Tanner, A.A. Komissarov, and S.L. Deutscher Crystal structure of an antigen-binding fragment bound to single-stranded DNA J. Mol. Biol. 314 2001 807 822
    • (2001) J. Mol. Biol. , vol.314 , pp. 807-822
    • Tanner, J.J.1    Komissarov, A.A.2    Deutscher, S.L.3
  • 37
    • 0029993902 scopus 로고    scopus 로고
    • Accessing the Kabat antibody sequence database by computer
    • A.C. Martin Accessing the Kabat antibody sequence database by computer Proteins: Struct. Funct. Genet 25 1996 130 133
    • (1996) Proteins: Struct. Funct. Genet , vol.25 , pp. 130-133
    • Martin, A.C.1
  • 38
    • 13044254231 scopus 로고    scopus 로고
    • Analysis and characterization of data from twinned crystals
    • N. Chandra, K.R. Acharya, and P.C. Moody Analysis and characterization of data from twinned crystals Acta Crystallog. sect. D 55 1999 1750 1758
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 1750-1758
    • Chandra, N.1    Acharya, K.R.2    Moody, P.C.3
  • 39
    • 0242713120 scopus 로고    scopus 로고
    • Twinned crystals and anomalous phasing
    • Z. Dauter Twinned crystals and anomalous phasing Acta Crystallog. sect. D 59 2003 2004 2016
    • (2003) Acta Crystallog. Sect. D , vol.59 , pp. 2004-2016
    • Dauter, Z.1
  • 40
    • 0242544104 scopus 로고    scopus 로고
    • Introduction to twinning
    • S. Parsons Introduction to twinning Acta Crystallog. sect. D 59 2003 1995 2003
    • (2003) Acta Crystallog. Sect. D , vol.59 , pp. 1995-2003
    • Parsons, S.1
  • 41
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • T.O. Yeates Detecting and overcoming crystal twinning Methods Enzymol. 276 1997 344 358
    • (1997) Methods Enzymol. , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 42
    • 0033081404 scopus 로고    scopus 로고
    • Protein crystals and their evil twins
    • T.O. Yeates, and B.C. Fam Protein crystals and their evil twins Struct. Fold. Des. 7 1999 R25 R29
    • (1999) Struct. Fold. Des. , vol.7
    • Yeates, T.O.1    Fam, B.C.2
  • 43
    • 12144290520 scopus 로고    scopus 로고
    • Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120
    • C.C. Huang, M. Venturi, S. Majeed, M.J. Moore, S. Phogat, and M.Y. Zhang Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120 Proc. Natl Acad. Sci. USA 101 2004 2706 2711
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2706-2711
    • Huang, C.C.1    Venturi, M.2    Majeed, S.3    Moore, M.J.4    Phogat, S.5    Zhang, M.Y.6
  • 44
    • 0032500701 scopus 로고    scopus 로고
    • A comparison of the crystallographic structures of two catalytic antibodies with esterase activity
    • J.L. Buchbinder, R.C. Stephenson, T.S. Scanlan, and R.J. Fletterick A comparison of the crystallographic structures of two catalytic antibodies with esterase activity J. Mol. Biol. 282 1998 1033 1041
    • (1998) J. Mol. Biol. , vol.282 , pp. 1033-1041
    • Buchbinder, J.L.1    Stephenson, R.C.2    Scanlan, T.S.3    Fletterick, R.J.4
  • 45
    • 4544339404 scopus 로고    scopus 로고
    • Structure of an anti-DNA fab complexed with a non-DNA ligand provides insights into cross-reactivity and molecular mimicry
    • J.P. Schuermann, M.T. Henzl, S.L. Deutscher, and J.J. Tanner Structure of an anti-DNA fab complexed with a non-DNA ligand provides insights into cross-reactivity and molecular mimicry Proteins: Struct. Funct. Genet. 57 2004 269 278
    • (2004) Proteins: Struct. Funct. Genet. , vol.57 , pp. 269-278
    • Schuermann, J.P.1    Henzl, M.T.2    Deutscher, S.L.3    Tanner, J.J.4
  • 46
  • 47
    • 0030821164 scopus 로고    scopus 로고
    • Structural insights into the evolution of an antibody combining site
    • G.J. Wedemayer, P.A. Patten, L.H. Wang, P.G. Schultz, and R.C. Stevens Structural insights into the evolution of an antibody combining site Science 276 1997 1665 1669
    • (1997) Science , vol.276 , pp. 1665-1669
    • Wedemayer, G.J.1    Patten, P.A.2    Wang, L.H.3    Schultz, P.G.4    Stevens, R.C.5
  • 48
    • 0037634024 scopus 로고    scopus 로고
    • Changes in structure and dynamics of the Fv fragment of a catalytic antibody upon binding of inhibitor
    • G.J. Kroon, H. Mo, M.A. Martinez-Yamout, H.J. Dyson, and P.E. Wright Changes in structure and dynamics of the Fv fragment of a catalytic antibody upon binding of inhibitor Protein Sci. 12 2003 1386 1394
    • (2003) Protein Sci. , vol.12 , pp. 1386-1394
    • Kroon, G.J.1    Mo, H.2    Martinez-Yamout, M.A.3    Dyson, H.J.4    Wright, P.E.5
  • 49
    • 0037435599 scopus 로고    scopus 로고
    • Dissection of binding interactions in the complex between the anti-lysozyme antibody HyHEL-63 and its antigen
    • Y. Li, M. Urrutia, S.J. Smith-Gill, and R.A. Mariuzza Dissection of binding interactions in the complex between the anti-lysozyme antibody HyHEL-63 and its antigen Biochemistry 42 2003 11 22
    • (2003) Biochemistry , vol.42 , pp. 11-22
    • Li, Y.1    Urrutia, M.2    Smith-Gill, S.J.3    Mariuzza, R.A.4
  • 50
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • A.J. Doig, and M.J. Sternberg Side-chain conformational entropy in protein folding Protein Sci. 4 1995 2247 2251
    • (1995) Protein Sci. , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, M.J.2
  • 51
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • B.W. Matthews, H. Nicholson, and W.J. Becktel Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding Proc. Natl Acad. Sci. USA 84 1987 6663 6667
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 52
    • 0026714968 scopus 로고
    • Role of proline residues in human lysozyme stability: A scanning calorimetric study combined with X-ray structure analysis of proline mutants
    • T. Herning, K. Yutani, K. Inaka, R. Kuroki, M. Matsushima, and M. Kikuchi Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants Biochemistry 31 1992 7077 7085
    • (1992) Biochemistry , vol.31 , pp. 7077-7085
    • Herning, T.1    Yutani, K.2    Inaka, K.3    Kuroki, R.4    Matsushima, M.5    Kikuchi, M.6
  • 53
  • 54
    • 0031468694 scopus 로고    scopus 로고
    • Effect of introducing proline residues on the stability of Aspergillus awamori
    • Y. Li, P.J. Reilly, and C. Ford Effect of introducing proline residues on the stability of Aspergillus awamori Protein Eng. 10 1997 1199 1204
    • (1997) Protein Eng. , vol.10 , pp. 1199-1204
    • Li, Y.1    Reilly, P.J.2    Ford, C.3
  • 55
    • 0016207522 scopus 로고
    • Binding of 2,4-dinitrophenyl compounds and other small molecules to a crystalline lambda-type Bence-Jones dimer
    • A.B. Edmundson, K.R. Ely, R.L. Girling, E.E. Abola, M. Schiffer, and F.A. Westholm Binding of 2,4-dinitrophenyl compounds and other small molecules to a crystalline lambda-type Bence-Jones dimer Biochemistry 13 1974 3816 3827
    • (1974) Biochemistry , vol.13 , pp. 3816-3827
    • Edmundson, A.B.1    Ely, K.R.2    Girling, R.L.3    Abola, E.E.4    Schiffer, M.5    Westholm, F.A.6
  • 57
    • 0027133936 scopus 로고
    • Detailed analysis of the free and bound conformations of an antibody. X-ray structures of Fab 17/9 and three different Fab-peptide complexes
    • U. Schulze-Gahmen, J.M. Rini, and I.A. Wilson Detailed analysis of the free and bound conformations of an antibody. X-ray structures of Fab 17/9 and three different Fab-peptide complexes J. Mol. Biol. 234 1993 1098 1118
    • (1993) J. Mol. Biol. , vol.234 , pp. 1098-1118
    • Schulze-Gahmen, U.1    Rini, J.M.2    Wilson, I.A.3
  • 58
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • J.M. Rini, U. Schulze-Gahmen, and I.A. Wilson Structural evidence for induced fit as a mechanism for antibody-antigen recognition Science 255 1992 959 965
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 59
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • I.A. Wilson, and R.L. Stanfield Antibody-antigen interactions: new structures and new conformational changes Curr. Opin. Struct. Biol. 4 1994 857 867
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 60
    • 0027943261 scopus 로고
    • Conformational isomerism and the diversity of antibodies
    • J. Foote, and C. Milstein Conformational isomerism and the diversity of antibodies Proc. Natl Acad. Sci. USA 91 1994 10370 10374
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10370-10374
    • Foote, J.1    Milstein, C.2
  • 61
    • 0027438239 scopus 로고
    • Construction, characterization, and selected site-specific mutagenesis of an anti-single-stranded DNA single chain autoantibody
    • C.A. Rumbley, L.K. Denzin, L. Yantz, S.Y. Tetin, and E.W. Voss Jr Construction, characterization, and selected site-specific mutagenesis of an anti-single-stranded DNA single chain autoantibody J. Biol. Chem. 268 1993 13667 13674
    • (1993) J. Biol. Chem. , vol.268 , pp. 13667-13674
    • Rumbley, C.A.1    Denzin, L.K.2    Yantz, L.3    Tetin, S.Y.4    Voss Jr., E.W.5
  • 62
    • 0027860511 scopus 로고
    • Elucidation of anti-ssDNA autoantibody BV 04-01 binding interactions with homooligonucleotides
    • S.Y. Tetin, C.A. Rumbley, T.L. Hazlett, and E.W. Voss Jr Elucidation of anti-ssDNA autoantibody BV 04-01 binding interactions with homooligonucleotides Biochemistry 32 1993 9011 9017
    • (1993) Biochemistry , vol.32 , pp. 9011-9017
    • Tetin, S.Y.1    Rumbley, C.A.2    Hazlett, T.L.3    Voss Jr., E.W.4
  • 63
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • H.J. Dyson, and P.E. Wright Coupling of folding and binding for unstructured proteins Curr. Opin. Struct. Biol. 12 2002 54 60
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 64
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • P.E. Wright, and H.J. Dyson Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm J. Mol. Biol. 293 1999 321 331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 65
    • 0031031915 scopus 로고    scopus 로고
    • High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA
    • M.A. Markus, A.P. Hinck, S. Huang, D.E. Draper, and D.A. Torchia High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA Nature Struct. Biol. 4 1997 70 77
    • (1997) Nature Struct. Biol. , vol.4 , pp. 70-77
    • Markus, M.A.1    Hinck, A.P.2    Huang, S.3    Draper, D.E.4    Torchia, D.A.5
  • 66
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • L.C. James, P. Roversi, and D.S. Tawfik Antibody multispecificity mediated by conformational diversity Science 299 2003 1362 1367
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 67
    • 0037470415 scopus 로고    scopus 로고
    • Immunology. Isomeric antibodies
    • J. Foote Immunology. Isomeric antibodies Science 299 2003 1327 1328
    • (2003) Science , vol.299 , pp. 1327-1328
    • Foote, J.1
  • 68
    • 0033869038 scopus 로고    scopus 로고
    • Crystallization and molecular replacement studies of a recombinant antigen-binding fragment complexed with single-stranded DNA
    • S.P. Prewitt, A.A. Komissarov, S.L. Deutscher, and J.J. Tanner Crystallization and molecular replacement studies of a recombinant antigen-binding fragment complexed with single-stranded DNA Acta Crystallog. sect. D 56 2000 1007 1011
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 1007-1011
    • Prewitt, S.P.1    Komissarov, A.A.2    Deutscher, S.L.3    Tanner, J.J.4
  • 69
    • 0141959921 scopus 로고    scopus 로고
    • MRSAD: Using anomalous dispersion from S atoms collected at Cu Kalpha wavelength in molecular-replacement structure determination
    • J.P. Schuermann, and J.J. Tanner MRSAD: using anomalous dispersion from S atoms collected at Cu Kalpha wavelength in molecular-replacement structure determination Acta Crystallog. sect. D 59 2003 1731 1736
    • (2003) Acta Crystallog. Sect. D , vol.59 , pp. 1731-1736
    • Schuermann, J.P.1    Tanner, J.J.2
  • 70
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 71
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • J. Navaza Implementation of molecular replacement in AMoRe Acta Crystallog. sect. D 57 2001 1367 1372
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 73
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 74
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • M.D. Winn, G.N. Murshudov, and M.Z. Papiz Macromolecular TLS refinement in REFMAC at moderate resolutions Methods Enzymol. 374 2003 300 321
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 75
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallog. sect. D 57 2001 122 133
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 76
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 77
    • 12644299138 scopus 로고
    • Solvent model for protein crystals: On occupancy parameters for discrete solvent sites and the solvent continuum
    • L.H. Jensen Solvent model for protein crystals: on occupancy parameters for discrete solvent sites and the solvent continuum Acta Crystallog. sect. B 46 1990 650 653
    • (1990) Acta Crystallog. Sect. B , vol.46 , pp. 650-653
    • Jensen, L.H.1
  • 78
    • 0001638309 scopus 로고
    • The influence of twinning by merohedry on intensity statistics
    • D.C. Rees The influence of twinning by merohedry on intensity statistics Acta Crystallog. sect. A 36 1980 578 581
    • (1980) Acta Crystallog. Sect. a , vol.36 , pp. 578-581
    • Rees, D.C.1
  • 79
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 80
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • H. Luecke, H.T. Richter, and J.K. Lanyi Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution Science 280 1998 1934 1937
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 82
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for x-ray protein structure refinement
    • R.A. Engh, and R. Huber Accurate bond and angle parameters for x-ray protein structure refinement Acta Crystallog. sect. A 47 1991 392 400
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 83


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