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Volumn 83, Issue 8, 2015, Pages 1385-1406

AbDesign: An algorithm for combinatorial backbone design guided by natural conformations and sequences

Author keywords

Canonical conformations; CDRs; Computational protein design; Conformation sequence optimization; Fuzzy logic design; Modular segments; Rosetta; V(D)J recombination

Indexed keywords

ANTIBODY; EPITOPE; COMPLEMENTARITY DETERMINING REGION;

EID: 84937736814     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24779     Document Type: Article
Times cited : (94)

References (113)
  • 1
    • 36448933773 scopus 로고    scopus 로고
    • A de novo designed protein protein interface
    • Huang PS, Love JJ, Mayo SL. A de novo designed protein protein interface. Protein Sci 2007;16:2770-2774.
    • (2007) Protein Sci , vol.16 , pp. 2770-2774
    • Huang, P.S.1    Love, J.J.2    Mayo, S.L.3
  • 5
    • 84892615437 scopus 로고    scopus 로고
    • Computational design of a pH-sensitive IgG binding protein
    • Strauch EM, Fleishman SJ, Baker D. Computational design of a pH-sensitive IgG binding protein. Proc Natl Acad Sci USA 2014;111:675-680.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 675-680
    • Strauch, E.M.1    Fleishman, S.J.2    Baker, D.3
  • 12
    • 84855685292 scopus 로고    scopus 로고
    • Metal-mediated affinity and orientation specificity in a computationally designed protein homodimer
    • Der BS, Machius M, Miley MJ, Mills JL, Szyperski T, Kuhlman B. Metal-mediated affinity and orientation specificity in a computationally designed protein homodimer. J Am Chem Soc 2012;134:375-385.
    • (2012) J Am Chem Soc , vol.134 , pp. 375-385
    • Der, B.S.1    Machius, M.2    Miley, M.J.3    Mills, J.L.4    Szyperski, T.5    Kuhlman, B.6
  • 13
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L, Chothia C, Janin J. The atomic structure of protein-protein recognition sites. J Mol Biol 1999;285:2177-2198.
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 16
    • 84873024403 scopus 로고    scopus 로고
    • A comparison of successful and failed protein interface designs highlights the challenges of designing buried hydrogen bonds
    • Stranges PB, Kuhlman B. A comparison of successful and failed protein interface designs highlights the challenges of designing buried hydrogen bonds. Protein Sci 2013;22:74-82.
    • (2013) Protein Sci , vol.22 , pp. 74-82
    • Stranges, P.B.1    Kuhlman, B.2
  • 17
    • 84876020987 scopus 로고    scopus 로고
    • Emerging themes in the computational design of novel enzymes and protein-protein interfaces
    • Khare SD, Fleishman SJ. Emerging themes in the computational design of novel enzymes and protein-protein interfaces. FEBS Lett 2013;587:1147-1154.
    • (2013) FEBS Lett , vol.587 , pp. 1147-1154
    • Khare, S.D.1    Fleishman, S.J.2
  • 18
    • 84859765617 scopus 로고    scopus 로고
    • Role of the biomolecular energy gap in protein design, structure, and evolution
    • Fleishman SJ, Baker D. Role of the biomolecular energy gap in protein design, structure, and evolution. Cell 2012;149:262-273.
    • (2012) Cell , vol.149 , pp. 262-273
    • Fleishman, S.J.1    Baker, D.2
  • 21
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of bence jones proteins and myeloma light chains and their implications for antibody complementarity
    • Wu, T, Te Kabat, E. An analysis of the sequences of the variable regions of bence jones proteins and myeloma light chains and their implications for antibody complementarity. J Exp Med 1970;132:211-250.
    • (1970) J Exp Med , vol.132 , pp. 211-250
    • Wu, T.1    Te Kabat, E.2
  • 22
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C, Lesk AM. Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol 1987;196:901-917.
    • (1987) J Mol Biol , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 23
    • 0015146402 scopus 로고
    • A homologous series of affinity labeling reagents and their use in the study of antibody binding sites
    • Strausbauch PH, Weinstein Y, Wilchek M, Shaltiel S, Givol D. A homologous series of affinity labeling reagents and their use in the study of antibody binding sites. Biochemistry 1971;10:4342-4348.
    • (1971) Biochemistry , vol.10 , pp. 4342-4348
    • Strausbauch, P.H.1    Weinstein, Y.2    Wilchek, M.3    Shaltiel, S.4    Givol, D.5
  • 24
    • 79251598995 scopus 로고    scopus 로고
    • A new clustering of antibody CDR loop conformations
    • North B, Lehmann A, Dunbrack RL. A new clustering of antibody CDR loop conformations. J Mol Biol 2011;406:228-256.
    • (2011) J Mol Biol , vol.406 , pp. 228-256
    • North, B.1    Lehmann, A.2    Dunbrack, R.L.3
  • 25
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani B, Lesk AM, Chothia C. Standard conformations for the canonical structures of immunoglobulins. J Mol Biol 1997;273:927-948.
    • (1997) J Mol Biol , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 27
    • 0017747498 scopus 로고
    • Unusual distributions of amino acids in complementarity-determining (hypervariable) segments of heavy and light chains of immunoglobulins and their possible roles in specificity of antibody-combining sites
    • Kabat EA, Wu TT, Bilofsky H. Unusual distributions of amino acids in complementarity-determining (hypervariable) segments of heavy and light chains of immunoglobulins and their possible roles in specificity of antibody-combining sites. J Biol Chem 1977;252:6609-6616.
    • (1977) J Biol Chem , vol.252 , pp. 6609-6616
    • Kabat, E.A.1    Wu, T.T.2    Bilofsky, H.3
  • 28
    • 84879549646 scopus 로고    scopus 로고
    • What makes a protein fold amenable to functional innovation? Fold polarity and stability trade-offs
    • Dellus-Gur E, Toth-Petroczy A, Elias M, Tawfik DS. What makes a protein fold amenable to functional innovation? Fold polarity and stability trade-offs. J Mol Biol 2013;425:2609-2621.
    • (2013) J Mol Biol , vol.425 , pp. 2609-2621
    • Dellus-Gur, E.1    Toth-Petroczy, A.2    Elias, M.3    Tawfik, D.S.4
  • 29
    • 0020429363 scopus 로고
    • Evolution of proteins formed by β-sheets: II. The core of the immunoglobulin domains
    • Lesk A, Chothia C. Evolution of proteins formed by β-sheets: II. The core of the immunoglobulin domains. J Mol Biol 1982;160:325-342.
    • (1982) J Mol Biol , vol.160 , pp. 325-342
    • Lesk, A.1    Chothia, C.2
  • 31
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones P, Dear P, Foote J, Neuberger M, Winter G. Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 1986;321:522-525.
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.1    Dear, P.2    Foote, J.3    Neuberger, M.4    Winter, G.5
  • 32
    • 0025978976 scopus 로고
    • Man-made antibodies
    • Winter G, Milstein C. Man-made antibodies. Nature 1991;349:293-299.
    • (1991) Nature , vol.349 , pp. 293-299
    • Winter, G.1    Milstein, C.2
  • 33
    • 43749108590 scopus 로고    scopus 로고
    • Submitting antibodies to binding arbitration
    • Michnick SW, Sidhu SS. Submitting antibodies to binding arbitration. Nat Chem Biol 2008;4:326-329.
    • (2008) Nat Chem Biol , vol.4 , pp. 326-329
    • Michnick, S.W.1    Sidhu, S.S.2
  • 34
    • 77951586447 scopus 로고    scopus 로고
    • Strategies and challenges for the next generation of therapeutic antibodies
    • Beck A, Wurch T, Bailly C, Corvaia N. Strategies and challenges for the next generation of therapeutic antibodies. Nat Rev Immunol 2010;10:345-352.
    • (2010) Nat Rev Immunol , vol.10 , pp. 345-352
    • Beck, A.1    Wurch, T.2    Bailly, C.3    Corvaia, N.4
  • 35
    • 34248551662 scopus 로고    scopus 로고
    • Antibody engineering and modification technologies
    • Filpula D. Antibody engineering and modification technologies. Biomol Eng 2007;24:201-215.
    • (2007) Biomol Eng , vol.24 , pp. 201-215
    • Filpula, D.1
  • 37
    • 84859510667 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies against influenza virus and prospects for universal therapies
    • Ekiert DC, Wilson IA. Broadly neutralizing antibodies against influenza virus and prospects for universal therapies. Curr Opin Virol 2012;2:134-141.
    • (2012) Curr Opin Virol , vol.2 , pp. 134-141
    • Ekiert, D.C.1    Wilson, I.A.2
  • 38
    • 0033855859 scopus 로고    scopus 로고
    • Clinical trials of antibody therapy
    • Glennie MJ, Johnson PW. Clinical trials of antibody therapy. Immunol Today 2000;21:403-410.
    • (2000) Immunol Today , vol.21 , pp. 403-410
    • Glennie, M.J.1    Johnson, P.W.2
  • 39
    • 0037022297 scopus 로고    scopus 로고
    • Conformational abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B, Wetzel R. Conformational abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci USA 2002;99:1485-1490.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 41
    • 9444277172 scopus 로고    scopus 로고
    • Single-chain antibodies for the conformation-specific blockade of activated platelet integrin alphaIIbbeta3 designed by subtractive selection from naive human phage libraries
    • Schwarz M, Röttgen P, Takada Y, Le Gall F, Knackmuss S, Bassler N, Büttner C, Little M, Bode C, Peter K. Single-chain antibodies for the conformation-specific blockade of activated platelet integrin alphaIIbbeta3 designed by subtractive selection from naive human phage libraries. FASEB J 2004;18:1704-1706.
    • (2004) FASEB J , vol.18 , pp. 1704-1706
    • Schwarz, M.1    Röttgen, P.2    Takada, Y.3    Le Gall, F.4    Knackmuss, S.5    Bassler, N.6    Büttner, C.7    Little, M.8    Bode, C.9    Peter, K.10
  • 46
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibody-affinity improvement beyond in vivo maturation
    • Lippow SM, Wittrup KD, Tidor B. Computational design of antibody-affinity improvement beyond in vivo maturation. Nat Biotechnol 2007;25:1171-1176.
    • (2007) Nat Biotechnol , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 49
    • 67649647815 scopus 로고    scopus 로고
    • Improving the species cross-reactivity of an antibody using computational design
    • Farady CJ, Sellers BD, Jacobson MP, Craik CS. Improving the species cross-reactivity of an antibody using computational design. Bioorg Med Chem Lett 2009;19:3744-3747.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 3744-3747
    • Farady, C.J.1    Sellers, B.D.2    Jacobson, M.P.3    Craik, C.S.4
  • 51
    • 77958157337 scopus 로고    scopus 로고
    • OptCDR: a general computational method for the design of antibody complementarity determining regions for targeted epitope binding
    • Pantazes RJ, Maranas CD. OptCDR: a general computational method for the design of antibody complementarity determining regions for targeted epitope binding. Protein Eng Des Sel 2010;23:849-858.
    • (2010) Protein Eng Des Sel , vol.23 , pp. 849-858
    • Pantazes, R.J.1    Maranas, C.D.2
  • 52
    • 84878255395 scopus 로고    scopus 로고
    • MAPs: a database of modular antibody parts for predicting tertiary structures and designing affinity matured antibodies
    • Pantazes RJ, Maranas CD. MAPs: a database of modular antibody parts for predicting tertiary structures and designing affinity matured antibodies. BMC Bioinform 2013;14:168.
    • (2013) BMC Bioinform , vol.14 , pp. 168
    • Pantazes, R.J.1    Maranas, C.D.2
  • 53
    • 84937737866 scopus 로고    scopus 로고
    • OptMAVEn-a new framework for the de novo design of antibody variable region models targeting specific antigen epitopes
    • Li T, Pantazes RJ, Maranas CD. OptMAVEn-a new framework for the de novo design of antibody variable region models targeting specific antigen epitopes. PLoS One 2014;9:e105954.
    • (2014) PLoS One , vol.9 , pp. e105954
    • Li, T.1    Pantazes, R.J.2    Maranas, C.D.3
  • 54
    • 50649095790 scopus 로고    scopus 로고
    • Macromolecular modeling with Rosetta
    • Das R, Baker D. Macromolecular modeling with Rosetta. Annu Rev Biochem 2008;77:363-382.
    • (2008) Annu Rev Biochem , vol.77 , pp. 363-382
    • Das, R.1    Baker, D.2
  • 56
    • 84874032378 scopus 로고    scopus 로고
    • Computational design of novel protein binders and experimental affinity maturation
    • Whitehead TA, Baker D, Fleishman SJ. Computational design of novel protein binders and experimental affinity maturation. Methods Enzymol 2013;523:1-19.
    • (2013) Methods Enzymol , vol.523 , pp. 1-19
    • Whitehead, T.A.1    Baker, D.2    Fleishman, S.J.3
  • 57
    • 0038021436 scopus 로고    scopus 로고
    • Assessment of blind predictions of protein-protein interactions: current status of docking methods
    • Méndez R, Leplae R, De Maria L, Wodak SJ. Assessment of blind predictions of protein-protein interactions: current status of docking methods. Proteins 2003;52:51-67.
    • (2003) Proteins , vol.52 , pp. 51-67
    • Méndez, R.1    Leplae, R.2    De Maria, L.3    Wodak, S.J.4
  • 58
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence MC, Colman PM. Shape complementarity at protein/protein interfaces. J Mol Biol 1993;234:946-950.
    • (1993) J Mol Biol , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 59
    • 58149463441 scopus 로고    scopus 로고
    • RosettaHoles: rapid assessment of protein core packing for structure prediction, refinement, design, and validation
    • Sheffler W, Baker D. RosettaHoles: rapid assessment of protein core packing for structure prediction, refinement, design, and validation. Protein Sci 2009;18:229-239.
    • (2009) Protein Sci , vol.18 , pp. 229-239
    • Sheffler, W.1    Baker, D.2
  • 61
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations
    • Gray JJ, Moughon S, Wang C, Schueler-Furman O, Kuhlman B, Rohl CA, Baker D. Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations. J Mol Biol 2003;331:281-299.
    • (2003) J Mol Biol , vol.331 , pp. 281-299
    • Gray, J.J.1    Moughon, S.2    Wang, C.3    Schueler-Furman, O.4    Kuhlman, B.5    Rohl, C.A.6    Baker, D.7
  • 62
    • 79953169868 scopus 로고    scopus 로고
    • Restricted sidechain plasticity in the structures of native proteins and complexes
    • Fleishman SJ, Khare SD, Koga N, Baker D. Restricted sidechain plasticity in the structures of native proteins and complexes. Protein Sci 2011;20:753-757.
    • (2011) Protein Sci , vol.20 , pp. 753-757
    • Fleishman, S.J.1    Khare, S.D.2    Koga, N.3    Baker, D.4
  • 63
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for binding energy hot spots in protein-protein complexes
    • Kortemme T, Baker D. A simple physical model for binding energy hot spots in protein-protein complexes. Proc Natl Acad Sci USA 2002;99:14116-14121.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14116-14121
    • Kortemme, T.1    Baker, D.2
  • 64
    • 0033058759 scopus 로고    scopus 로고
    • H3-rules: identification of CDR-H3 structures in antibodies
    • Shirai H, Kidera A, Nakamura H. H3-rules: identification of CDR-H3 structures in antibodies. FEBS Lett 1999;455:188-197.
    • (1999) FEBS Lett , vol.455 , pp. 188-197
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 65
    • 0024844388 scopus 로고
    • Conformations of immunoglobulin hypervariable regions
    • Chothia C, Lesk A, Tramontano A. Conformations of immunoglobulin hypervariable regions. Nature 1989.
    • (1989) Nature
    • Chothia, C.1    Lesk, A.2    Tramontano, A.3
  • 66
    • 79953815754 scopus 로고    scopus 로고
    • Bcl:: Cluster: a method for clustering biological molecules coupled with visualization in the Pymol Molecular Graphics System
    • 2011 IEEE 1st Int. Conf.
    • Alexander N, Woetzel N, Meiler J. Bcl:: Cluster: a method for clustering biological molecules coupled with visualization in the Pymol Molecular Graphics System. Comput Adv Biol Med Sci (ICCABS), 2011 IEEE 1st Int. Conf. 2011;13-18.
    • (2011) Comput Adv Biol Med Sci (ICCABS) , pp. 13-18
    • Alexander, N.1    Woetzel, N.2    Meiler, J.3
  • 67
    • 62649147821 scopus 로고    scopus 로고
    • Sequence context-specific profiles for homology searching
    • Biegert A, Söding J. Sequence context-specific profiles for homology searching. Proc Natl Acad Sci USA 2009;106:3770-3775.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3770-3775
    • Biegert, A.1    Söding, J.2
  • 69
    • 84914127473 scopus 로고    scopus 로고
    • "fuzzy"-logic language for encoding multiple physical traits in biomolecules
    • Warszawski S, Netzer R, Tawfik DS, Fleishman SJ. A "fuzzy"-logic language for encoding multiple physical traits in biomolecules. J Mol Biol 2014;426:4125-4138.
    • (2014) J Mol Biol , vol.426 , pp. 4125-4138
    • Warszawski, S.1    Netzer, R.2    Tawfik, D.S.3    Fleishman, S.A.4
  • 70
    • 34047232678 scopus 로고    scopus 로고
    • Positive and negative design in stability and thermal adaptation of natural proteins
    • Berezovsky IN, Zeldovich KB, Shakhnovich EI. Positive and negative design in stability and thermal adaptation of natural proteins. PLoS Comput Biol 2007;3:e52.
    • (2007) PLoS Comput Biol , vol.3 , pp. e52
    • Berezovsky, I.N.1    Zeldovich, K.B.2    Shakhnovich, E.I.3
  • 72
    • 68349104348 scopus 로고    scopus 로고
    • Sub-angstrom accuracy in protein loop reconstruction by robotics-inspired conformational sampling
    • Mandell D, Coutsias E, Kortemme T. Sub-angstrom accuracy in protein loop reconstruction by robotics-inspired conformational sampling. Nat Methods 2009;6:551-552.
    • (2009) Nat Methods , vol.6 , pp. 551-552
    • Mandell, D.1    Coutsias, E.2    Kortemme, T.3
  • 73
    • 45649084560 scopus 로고    scopus 로고
    • Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction
    • Smith CA, Kortemme T. Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction. J Mol Biol 2008;380:742-756.
    • (2008) J Mol Biol , vol.380 , pp. 742-756
    • Smith, C.A.1    Kortemme, T.2
  • 74
    • 0037406075 scopus 로고    scopus 로고
    • Cyclic coordinate descent: a robotics algorithm for protein loop closure
    • Canutescu AA, Jr, Dunbrack RL. Cyclic coordinate descent: a robotics algorithm for protein loop closure. Protein Sci 2003;12:963-972.
    • (2003) Protein Sci , vol.12 , pp. 963-972
    • Canutescu, A.A.1    Dunbrack, R.L.2
  • 78
    • 4744369286 scopus 로고    scopus 로고
    • Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody
    • Midelfort KS, Hernandez HH, Lippow SM, Tidor B, Drennan CL, Wittrup KD. Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody. J Mol Biol 2004;343:685-701.
    • (2004) J Mol Biol , vol.343 , pp. 685-701
    • Midelfort, K.S.1    Hernandez, H.H.2    Lippow, S.M.3    Tidor, B.4    Drennan, C.L.5    Wittrup, K.D.6
  • 80
    • 0017614064 scopus 로고
    • Structural basis for the specificity of antibody-antigen reactions and structural mechanisms for the diversification of antigen-binding specificities
    • Padlan EA. Structural basis for the specificity of antibody-antigen reactions and structural mechanisms for the diversification of antigen-binding specificities. Q Rev Biophys 1977;10:35-65.
    • (1977) Q Rev Biophys , vol.10 , pp. 35-65
    • Padlan, E.A.1
  • 81
    • 0027253021 scopus 로고
    • Optimal humanization of 1B4, an anti-CD18 murine monoclonal antibody, is achieved by correct choice of human V-region framework sequences
    • Singer I, et al. Optimal humanization of 1B4, an anti-CD18 murine monoclonal antibody, is achieved by correct choice of human V-region framework sequences. J Immunol 1993;150:2844-2857.
    • (1993) J Immunol , vol.150 , pp. 2844-2857
    • Singer, I.1
  • 82
    • 0025848797 scopus 로고
    • A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties
    • Padlan E. A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties. Mol Immunol 1991;28:489-498.
    • (1991) Mol Immunol , vol.28 , pp. 489-498
    • Padlan, E.1
  • 83
    • 0025063143 scopus 로고
    • Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins
    • Tramontano A, Chothia C, Lesk AM. Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins. J Mol Biol 1990;215:175-182.
    • (1990) J Mol Biol , vol.215 , pp. 175-182
    • Tramontano, A.1    Chothia, C.2    Lesk, A.M.3
  • 84
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote J, Winter G. Antibody framework residues affecting the conformation of the hypervariable loops. J Mol Biol 1992;224:487-499.
    • (1992) J Mol Biol , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 85
    • 0030577371 scopus 로고    scopus 로고
    • Structural classification of CDR-H3 in antibodies
    • Shirai H, Kidera A, Nakamura H. Structural classification of CDR-H3 in antibodies. FEBS Lett 1996;399:1-8.
    • (1996) FEBS Lett , vol.399 , pp. 1-8
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 87
    • 84894929772 scopus 로고    scopus 로고
    • Computational design of protein-small molecule interfaces
    • Allison B, et al. Computational design of protein-small molecule interfaces. J Struct Biol 2014;185:193-202.
    • (2014) J Struct Biol , vol.185 , pp. 193-202
    • Allison, B.1
  • 88
    • 84863774072 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses
    • Burton DR, Poignard P, Stanfield RL, Wilson IA. Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses. Science 2012;337:183-186.
    • (2012) Science , vol.337 , pp. 183-186
    • Burton, D.R.1    Poignard, P.2    Stanfield, R.L.3    Wilson, I.A.4
  • 94
    • 0035412387 scopus 로고    scopus 로고
    • Structure of a factor VIII C2 domain-immunoglobulin G4kappa fab complex: identification of an inhibitory antibody epitope on the surface of factor VIII
    • Spiegel PC. Structure of a factor VIII C2 domain-immunoglobulin G4kappa fab complex: identification of an inhibitory antibody epitope on the surface of factor VIII. Blood 2001;98:13-19.
    • (2001) Blood , vol.98 , pp. 13-19
    • Spiegel, P.C.1
  • 95
    • 0032516765 scopus 로고    scopus 로고
    • Structural basis for the binding of an anti-cytochrome c antibody to its antigen: crystal structures of FabE8-cytochrome c complex to 1.8 a resolution and FabE8 to 2.26 a resolution
    • Mylvaganam SE, Paterson Y, Getzoff ED. Structural basis for the binding of an anti-cytochrome c antibody to its antigen: crystal structures of FabE8-cytochrome c complex to 1.8 a resolution and FabE8 to 2.26 a resolution. J Mol Biol 1998;281:301-322.
    • (1998) J Mol Biol , vol.281 , pp. 301-322
    • Mylvaganam, S.E.1    Paterson, Y.2    Getzoff, E.D.3
  • 97
    • 1542408991 scopus 로고    scopus 로고
    • Structural mechanism for affinity maturation of an anti-lysozyme antibody
    • Cauerhff A, Goldbaum FA, Braden BC. Structural mechanism for affinity maturation of an anti-lysozyme antibody. Proc Natl Acad Sci USA 2004;101:3539-3544.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3539-3544
    • Cauerhff, A.1    Goldbaum, F.A.2    Braden, B.C.3
  • 98
    • 0032584379 scopus 로고    scopus 로고
    • The 2.5 a resolution structure of the jel42 fab fragment/HPr complex
    • Prasad L, Waygood EB, Lee JS, Delbaere LT. The 2.5 a resolution structure of the jel42 fab fragment/HPr complex. J Mol Biol 1998;280:829-845.
    • (1998) J Mol Biol , vol.280 , pp. 829-845
    • Prasad, L.1    Waygood, E.B.2    Lee, J.S.3    Delbaere, L.T.4
  • 100
    • 0035850666 scopus 로고    scopus 로고
    • The 1.85 a resolution crystal structures of tissue factor in complex with humanized fab D3h44 and of free humanized fab D3h44: revisiting the solvation of antigen combining sites
    • Faelber K, Kirchhofer D, Presta L, Kelley RF, Muller YA. The 1.85 a resolution crystal structures of tissue factor in complex with humanized fab D3h44 and of free humanized fab D3h44: revisiting the solvation of antigen combining sites. J Mol Biol 2001;313:83-97.
    • (2001) J Mol Biol , vol.313 , pp. 83-97
    • Faelber, K.1    Kirchhofer, D.2    Presta, L.3    Kelley, R.F.4    Muller, Y.A.5
  • 101
    • 0034641749 scopus 로고    scopus 로고
    • Native protein sequences are close to optimal for their structures
    • Kuhlman B, Baker D. Native protein sequences are close to optimal for their structures. Proc Natl Acad Sci USA 2000;97:10383-10388.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10383-10388
    • Kuhlman, B.1    Baker, D.2
  • 102
    • 0028429178 scopus 로고
    • Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains
    • Dunbrack RL, Karplus M. Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains. Nat Struct Mol Biol 1994;1:334-340.
    • (1994) Nat Struct Mol Biol , vol.1 , pp. 334-340
    • Dunbrack, R.L.1    Karplus, M.2
  • 103
    • 0035845637 scopus 로고    scopus 로고
    • A comparative analysis of the immunological evolution of antibody 28B4
    • Yin J, et al. A comparative analysis of the immunological evolution of antibody 28B4. Biochemistry 2001;40:10764-10773.
    • (2001) Biochemistry , vol.40 , pp. 10764-10773
    • Yin, J.1
  • 104
    • 0037373997 scopus 로고    scopus 로고
    • Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten
    • Sagawa T, Oda M, Ishimura M, Furukawa K, Azuma T. Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten. Mol Immunol 2003;39:801-808.
    • (2003) Mol Immunol , vol.39 , pp. 801-808
    • Sagawa, T.1    Oda, M.2    Ishimura, M.3    Furukawa, K.4    Azuma, T.5
  • 105
    • 0033634681 scopus 로고    scopus 로고
    • Maturation of an antibody response is governed by modulations in flexibility of the antigen-combining site
    • Manivel V, Sahoo NC, Salunke DM, Rao KV. Maturation of an antibody response is governed by modulations in flexibility of the antigen-combining site. Immunity 2000;13:611-620.
    • (2000) Immunity , vol.13 , pp. 611-620
    • Manivel, V.1    Sahoo, N.C.2    Salunke, D.M.3    Rao, K.V.4
  • 106
    • 0042744723 scopus 로고    scopus 로고
    • Structural plasticity and the evolution of antibody affinity and specificity
    • Yin J, Beuscher AE, Andryski SE, Stevens RC, Schultz PG. Structural plasticity and the evolution of antibody affinity and specificity. J Mol Biol 2003;330:651-656.
    • (2003) J Mol Biol , vol.330 , pp. 651-656
    • Yin, J.1    Beuscher, A.E.2    Andryski, S.E.3    Stevens, R.C.4    Schultz, P.G.5
  • 108
    • 70350334391 scopus 로고    scopus 로고
    • Computer-aided design of functional protein interactions
    • Mandell DJ, Kortemme T. Computer-aided design of functional protein interactions. Nat Chem Biol 2009;5:797-807.
    • (2009) Nat Chem Biol , vol.5 , pp. 797-807
    • Mandell, D.J.1    Kortemme, T.2
  • 109
    • 0026094165 scopus 로고
    • Humanization of a mouse monoclonal antibody by CDR-grafting: The importance of framework residues on loop conformation
    • Kettleborough CA, Saldanha J, Heath VJ, Morrison CJ, Bendig MM. Humanization of a mouse monoclonal antibody by CDR-grafting: The importance of framework residues on loop conformation. Protein Eng 1991;4:773-783.
    • (1991) Protein Eng , vol.4 , pp. 773-783
    • Kettleborough, C.A.1    Saldanha, J.2    Heath, V.J.3    Morrison, C.J.4    Bendig, M.M.5
  • 110
    • 0036785591 scopus 로고    scopus 로고
    • How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme?
    • Pons J, Stratton JR, Kirsch JF. How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme? Protein Sci 2002;11:2308-2315.
    • (2002) Protein Sci , vol.11 , pp. 2308-2315
    • Pons, J.1    Stratton, J.R.2    Kirsch, J.F.3
  • 111
    • 84878306995 scopus 로고    scopus 로고
    • Protein-protein interactions: general trends in the relationship between binding affinity and interfacial buried surface area
    • Chen J, Sawyer N, Regan L. Protein-protein interactions: general trends in the relationship between binding affinity and interfacial buried surface area. Protein Sci 2013;22:510-515.
    • (2013) Protein Sci , vol.22 , pp. 510-515
    • Chen, J.1    Sawyer, N.2    Regan, L.3


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