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Volumn 13, Issue 12, 2005, Pages 1775-1787

Structural basis of affinity maturation and intramolecular cooperativity in a protein-protein interaction

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AMINO ACID;

EID: 28844435898     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.08.015     Document Type: Article
Times cited : (40)

References (57)
  • 1
    • 0034607551 scopus 로고    scopus 로고
    • Evaluation of direct and cooperative contributions towards the strength of buried hydrogen bonds and salt bridges
    • S. Albeck, R. Unger, and G. Schreiber Evaluation of direct and cooperative contributions towards the strength of buried hydrogen bonds and salt bridges J. Mol. Biol. 298 2000 503 520
    • (2000) J. Mol. Biol. , vol.298 , pp. 503-520
    • Albeck, S.1    Unger, R.2    Schreiber, G.3
  • 2
    • 0025119206 scopus 로고
    • Three-dimensional structure determination of an anti-2-phenyloxazolone antibody: The role of somatic mutation and heavy/light chain pairing in the maturation of an immune response
    • P.M. Alzari, S. Spinelli, R.A. Mariuzza, G. Boulot, R.J. Poljak, J.M. Jarvis, and C. Milstein Three-dimensional structure determination of an anti-2-phenyloxazolone antibody: the role of somatic mutation and heavy/light chain pairing in the maturation of an immune response EMBO J. 9 1990 3807 3814
    • (1990) EMBO J. , vol.9 , pp. 3807-3814
    • Alzari, P.M.1    Spinelli, S.2    Mariuzza, R.A.3    Boulot, G.4    Poljak, R.J.5    Jarvis, J.M.6    Milstein, C.7
  • 3
    • 0035823601 scopus 로고    scopus 로고
    • Role of the T cell receptor ligand affinity in T cell activation by bacterial superantigens
    • P.S. Andersen, C. Geisler, S. Buus, R.A. Mariuzza, and K. Karjalainen Role of the T cell receptor ligand affinity in T cell activation by bacterial superantigens J. Biol. Chem. 276 2001 33452 33457
    • (2001) J. Biol. Chem. , vol.276 , pp. 33452-33457
    • Andersen, P.S.1    Geisler, C.2    Buus, S.3    Mariuzza, R.A.4    Karjalainen, K.5
  • 5
    • 0028956603 scopus 로고
    • Crystal structure of the β chain of a T cell antigen receptor
    • G.A. Bentley, G. Boulot, K. Karjalainen, and R.A. Mariuzza Crystal structure of the β chain of a T cell antigen receptor Science 267 1995 1984 1987
    • (1995) Science , vol.267 , pp. 1984-1987
    • Bentley, G.A.1    Boulot, G.2    Karjalainen, K.3    Mariuzza, R.A.4
  • 6
    • 2442660389 scopus 로고    scopus 로고
    • Dissecting the binding energy epitope of a high-affinity variant of human growth hormone: Cooperative and additive effects from combining mutations from independently selected phage display mutagenesis libraries
    • B. Bernat, M. Sun, M. Dwyer, M. Feldkamp, and A.A. Kossiakoff Dissecting the binding energy epitope of a high-affinity variant of human growth hormone: cooperative and additive effects from combining mutations from independently selected phage display mutagenesis libraries Biochemistry 43 2004 6076 6084
    • (2004) Biochemistry , vol.43 , pp. 6076-6084
    • Bernat, B.1    Sun, M.2    Dwyer, M.3    Feldkamp, M.4    Kossiakoff, A.A.5
  • 7
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • E.T. Boder, and K.D. Wittrup Yeast surface display for screening combinatorial polypeptide libraries Nat. Biotechnol. 15 1997 553 557
    • (1997) Nat. Biotechnol. , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 8
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • A.A. Bogan, and K.S. Thorn Anatomy of hot spots in protein interfaces J. Mol. Biol. 280 1998 1 9
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 9
    • 0033613074 scopus 로고    scopus 로고
    • Thermodynamics of T cell receptor binding to peptide-MHC: Evidence for a general mechanism of molecular scanning
    • J.J. Boniface, Z. Reich, D.S. Lyons, and M.M. Davis Thermodynamics of T cell receptor binding to peptide-MHC: evidence for a general mechanism of molecular scanning Proc. Natl. Acad. Sci. USA 96 1999 11446 11451
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11446-11451
    • Boniface, J.J.1    Reich, Z.2    Lyons, D.S.3    Davis, M.M.4
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 13
    • 0034610977 scopus 로고    scopus 로고
    • Mapping the energy of superantigen Staphylococcus enterotoxin C3 recognition of an α/β T cell receptor using alanine scanning mutagenesis
    • H.R. Churchill, P.S. Andersen, E.A. Parke, R.A. Mariuzza, and D.M. Kranz Mapping the energy of superantigen Staphylococcus enterotoxin C3 recognition of an α/β T cell receptor using alanine scanning mutagenesis J. Exp. Med. 191 2000 835 846
    • (2000) J. Exp. Med. , vol.191 , pp. 835-846
    • Churchill, H.R.1    Andersen, P.S.2    Parke, E.A.3    Mariuzza, R.A.4    Kranz, D.M.5
  • 14
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • L.L. Conte, C. Chothia, and J. Janin The atomic structure of protein-protein recognition sites J. Mol. Biol. 285 1999 2177 2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 17
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: Progress and challenges
    • W.L. DeLano Unraveling hot spots in binding interfaces: progress and challenges Curr. Opin. Struct. Biol. 12 2002 14 20
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 14-20
    • Delano, W.L.1
  • 18
    • 0033165928 scopus 로고    scopus 로고
    • Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
    • Y.H. Ding, B.M. Baker, D.N. Garboczi, W.E. Biddison, and D.C. Wiley Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical Immunity 11 1999 45 56
    • (1999) Immunity , vol.11 , pp. 45-56
    • Ding, Y.H.1    Baker, B.M.2    Garboczi, D.N.3    Biddison, W.E.4    Wiley, D.C.5
  • 20
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • K.C. Garcia, M. Degano, L.R. Pease, M. Huang, P.A. Peterson, L. Teyton, and I.A. Wilson Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen Science 279 1998 1166 1172
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1    Degano, M.2    Pease, L.R.3    Huang, M.4    Peterson, P.A.5    Teyton, L.6    Wilson, I.A.7
  • 21
    • 1042290495 scopus 로고    scopus 로고
    • Molecular interactions at the T cell-antigen-presenting cell interface
    • N.R. Gascoigne, and T. Zal Molecular interactions at the T cell-antigen-presenting cell interface Curr. Opin. Immunol. 16 2004 114 119
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 114-119
    • Gascoigne, N.R.1    Zal, T.2
  • 22
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • R. Guerois, J.E. Nielsen, and L. Serrano Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations J. Mol. Biol. 320 2002 369 387
    • (2002) J. Mol. Biol. , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 23
    • 0037079570 scopus 로고    scopus 로고
    • Computational alanine scanning of the 1:1 human growth hormone-receptor complex
    • S. Huo, I. Massova, and P.A. Kollman Computational alanine scanning of the 1:1 human growth hormone-receptor complex J. Comput. Chem. 23 2002 15 27
    • (2002) J. Comput. Chem. , vol.23 , pp. 15-27
    • Huo, S.1    Massova, I.2    Kollman, P.A.3
  • 24
    • 11844249426 scopus 로고    scopus 로고
    • Hot regions in protein-protein interactions: The organization and contribution of structurally conserved hot spot residues
    • O. Keskin, B. Ma, and R. Nussinov Hot regions in protein-protein interactions: the organization and contribution of structurally conserved hot spot residues J. Mol. Biol. 345 2005 1281 1294
    • (2005) J. Mol. Biol. , vol.345 , pp. 1281-1294
    • Keskin, O.1    Ma, B.2    Nussinov, R.3
  • 25
    • 0035853281 scopus 로고    scopus 로고
    • High affinity T cell receptors from yeast display libraries block T cell activation by superantigens
    • M.C. Kieke, E. Sundberg, E.V. Shusta, R.A. Mariuzza, K.D. Wittrup, and D.M. Kranz High affinity T cell receptors from yeast display libraries block T cell activation by superantigens J. Mol. Biol. 307 2001 1305 1315
    • (2001) J. Mol. Biol. , vol.307 , pp. 1305-1315
    • Kieke, M.C.1    Sundberg, E.2    Shusta, E.V.3    Mariuzza, R.A.4    Wittrup, K.D.5    Kranz, D.M.6
  • 26
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for binding energy hot spots in protein-protein complexes
    • T. Kortemme, and D. Baker A simple physical model for binding energy hot spots in protein-protein complexes Proc. Natl. Acad. Sci. USA 99 2002 14116 14121
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14116-14121
    • Kortemme, T.1    Baker, D.2
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0038103565 scopus 로고    scopus 로고
    • X-ray snapshots of the maturation of an antibody response to a protein antigen
    • Y. Li, H. Li, F. Yang, S.J. Smith-Gill, and R.A. Mariuzza X-ray snapshots of the maturation of an antibody response to a protein antigen Nat. Struct. Biol. 10 2003 482 488
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 482-488
    • Li, Y.1    Li, H.2    Yang, F.3    Smith-Gill, S.J.4    Mariuzza, R.A.5
  • 29
    • 13844272064 scopus 로고    scopus 로고
    • Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces
    • Y. Li, Y. Huang, C.P. Swaminathan, S.J. Smith-Gill, and R.A. Mariuzza Magnitude of the hydrophobic effect at central versus peripheral sites in protein-protein interfaces Structure (Camb.) 13 2005 297 307
    • (2005) Structure (Camb.) , vol.13 , pp. 297-307
    • Li, Y.1    Huang, Y.2    Swaminathan, C.P.3    Smith-Gill, S.J.4    Mariuzza, R.A.5
  • 30
    • 0030976150 scopus 로고    scopus 로고
    • Bacteriophage display and discovery of peptide leads for drug development
    • H.B. Lowman Bacteriophage display and discovery of peptide leads for drug development Annu. Rev. Biophys. Biomol. Struct. 26 1997 401 424
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 401-424
    • Lowman, H.B.1
  • 31
    • 0035366379 scopus 로고    scopus 로고
    • Protein functional epitopes: Hot spots, dynamics and combinatorial libraries
    • B. Ma, H.J. Wolfson, and R. Nussinov Protein functional epitopes: hot spots, dynamics and combinatorial libraries Curr. Opin. Struct. Biol. 11 2001 364 369
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 364-369
    • Ma, B.1    Wolfson, H.J.2    Nussinov, R.3
  • 32
    • 0033568644 scopus 로고    scopus 로고
    • Computational alanine scanning to probe protein-protein interactions: A novel approach to evaluate binding free energies
    • I. Massova, and P.A. Kollman Computational alanine scanning to probe protein-protein interactions: a novel approach to evaluate binding free energies J. Am. Chem. Soc. 121 1999 8133 8143
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8133-8143
    • Massova, I.1    Kollman, P.A.2
  • 33
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 34
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 35
    • 4744369286 scopus 로고    scopus 로고
    • Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody
    • K.S. Midelfort, H.H. Hernandez, S.M. Lippow, B. Tidor, C.L. Drennan, and K.D. Wittrup Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody J. Mol. Biol. 343 2004 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
  • 36
    • 0028835227 scopus 로고
    • Three-dimensional structures of the Fab fragment of murine N1G9 antibody from the primary immune response and of its complex with (4-hydroxy-3- nitrophenyl)acetate
    • R. Mizutani, K. Miura, T. Nakayama, I. Shimada, Y. Arata, and Y. Satow Three-dimensional structures of the Fab fragment of murine N1G9 antibody from the primary immune response and of its complex with (4-hydroxy-3-nitrophenyl) acetate J. Mol. Biol. 254 1995 208 222
    • (1995) J. Mol. Biol. , vol.254 , pp. 208-222
    • Mizutani, R.1    Miura, K.2    Nakayama, T.3    Shimada, I.4    Arata, Y.5    Satow, Y.6
  • 38
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • I.M. Nooren, and J.M. Thornton Diversity of protein-protein interactions EMBO J. 22 2003 3486 3492
    • (2003) EMBO J. , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing 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
  • 40
    • 14744305626 scopus 로고    scopus 로고
    • Intramolecular cooperativity in a protein binding site assessed by combinatorial shotgun scanning mutagenesis
    • G. Pal, M.H. Ultsch, K.P. Clark, B. Currell, A.A. Kossiakoff, and S.S. Sidhu Intramolecular cooperativity in a protein binding site assessed by combinatorial shotgun scanning mutagenesis J. Mol. Biol. 347 2005 489 494
    • (2005) J. Mol. Biol. , vol.347 , pp. 489-494
    • Pal, G.1    Ultsch, M.H.2    Clark, K.P.3    Currell, B.4    Kossiakoff, A.A.5    Sidhu, S.S.6
  • 41
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • T. Pawson, and P. Nash Protein-protein interactions define specificity in signal transduction Genes Dev. 14 2000 1027 1047
    • (2000) Genes Dev. , vol.14 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 45
    • 0032189032 scopus 로고    scopus 로고
    • Calculation of HyHel10-lysozyme binding free energy changes: Effect of ten point mutations
    • K.A. Sharp Calculation of HyHel10-lysozyme binding free energy changes: effect of ten point mutations Proteins 33 1998 39 48
    • (1998) Proteins , vol.33 , pp. 39-48
    • Sharp, K.A.1
  • 48
    • 0041333127 scopus 로고    scopus 로고
    • Structural, energetic and functional analysis of a protein-protein interface at distinct stages of affinity maturation
    • E.J. Sundberg, P.S. Andersen, P.M. Schlievert, K. Karjalainen, and R.A. Mariuzza Structural, energetic and functional analysis of a protein-protein interface at distinct stages of affinity maturation Structure 11 2003 1151 1161
    • (2003) Structure , vol.11 , pp. 1151-1161
    • Sundberg, E.J.1    Andersen, P.S.2    Schlievert, P.M.3    Karjalainen, K.4    Mariuzza, R.A.5
  • 49
    • 0037452522 scopus 로고    scopus 로고
    • Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2)
    • D.P. Teufel, R.Y. Kao, K.R. Acharya, and R. Shapiro Mutational analysis of the complex of human RNase inhibitor and human eosinophil-derived neurotoxin (RNase 2) Biochemistry 42 2003 1451 1459
    • (2003) Biochemistry , vol.42 , pp. 1451-1459
    • Teufel, D.P.1    Kao, R.Y.2    Acharya, K.R.3    Shapiro, R.4
  • 50
    • 0036468365 scopus 로고    scopus 로고
    • Eukaryotic transcription factors
    • A.J. Warren Eukaryotic transcription factors Curr. Opin. Struct. Biol. 12 2002 107 114
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 107-114
    • Warren, A.J.1
  • 51
    • 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
  • 54
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis of macromolecular recognition
    • S.J. Wodak, and J. Janin Structural basis of macromolecular recognition Adv. Protein Chem. 61 2002 9 73
    • (2002) Adv. Protein Chem. , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 55
    • 0033579560 scopus 로고    scopus 로고
    • Mutational analysis of the affinity maturation of antibody 48G7
    • P.L. Yang, and P.G. Schultz Mutational analysis of the affinity maturation of antibody 48G7 J. Mol. Biol. 294 1999 1191 1201
    • (1999) J. Mol. Biol. , vol.294 , pp. 1191-1201
    • Yang, P.L.1    Schultz, P.G.2
  • 57
    • 0028844323 scopus 로고
    • Structural analysis of affinity maturation: The three-dimensional structures of complexes of an anti-nitrophenol antibody
    • S.C. Yuhasz, C. Parry, M. Strand, and L.M. Amzel Structural analysis of affinity maturation: the three-dimensional structures of complexes of an anti-nitrophenol antibody Mol. Immunol. 32 1995 1143 1155
    • (1995) Mol. Immunol. , vol.32 , pp. 1143-1155
    • Yuhasz, S.C.1    Parry, C.2    Strand, M.3    Amzel, L.M.4


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