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Volumn 49, Issue 33, 2010, Pages 7050-7059

Combinations of affinity-enhancing mutations in a T cell receptor reveal highly nonadditive effects within and between complementarity determining regions and chains

Author keywords

[No Author keywords available]

Indexed keywords

ANTICOOPERATIVITY; ASSOCIATION RATES; BINDING AFFINITIES; BINDING KINETICS; COMPLEMENTARITY-DETERMINING REGIONS; COMPLEX NATURE; COOPERATIVE INTERACTIONS; COOPERATIVITY; DISSOCIATION RATES; FUTURE DESIGNS; IN-VITRO; IN-VIVO; MAJOR HISTOCOMPATIBILITY COMPLEX; MULTIPLE MUTATIONS; NON-ADDITIVE; POINT MUTATIONS; PROTEIN DESIGN; PROTEIN-PROTEIN INTERFACE; SIDE CHAINS; STRUCTURAL MODELING; STRUCTURAL RESPONSE; STRUCTURE-BASED DESIGNS; T CELL RECEPTOR; T-CELL RECEPTORS; TWO SOURCES; VIRAL PEPTIDES; WILD TYPES;

EID: 77955687387     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901969a     Document Type: Article
Times cited : (10)

References (47)
  • 1
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells, J. A. (1990) Additivity of mutational effects in proteins Biochemistry 29, 8509-8517
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 3
    • 33745227715 scopus 로고    scopus 로고
    • A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor
    • Kraich, M., Klein, M., Patino, E., Harrer, H., Nickel, J., Sebald, W., and Mueller, T. D. (2006) A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor BMC Biol. 4, 13
    • (2006) BMC Biol. , vol.4 , pp. 13
    • Kraich, M.1    Klein, M.2    Patino, E.3    Harrer, H.4    Nickel, J.5    Sebald, W.6    Mueller, T.D.7
  • 4
    • 38049029758 scopus 로고    scopus 로고
    • The modular organization of domain structures: Insights into protein-protein binding
    • del Sol, A. and Carbonell, P. (2007) The modular organization of domain structures: Insights into protein-protein binding PLoS Comput. Biol. 3, e239
    • (2007) PLoS Comput. Biol. , vol.3 , pp. 239
    • Del Sol, A.1    Carbonell, P.2
  • 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
    • Bernat, B., Sun, M., Dwyer, M., Feldkamp, M., and Kossiakoff, A. A. (2004) 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, 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
  • 8
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibody-affinity improvement beyond in vivo maturation
    • Lippow, S. M., Wittrup, K. D., and Tidor, B. (2007) Computational design of antibody-affinity improvement beyond in vivo maturation Nat. Biotechnol. 25, 1171-1176
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 10
    • 21044436808 scopus 로고    scopus 로고
    • Insights into peptide-based vaccine design for cancer immunotherapy
    • Lazoura, E. and Apostolopoulos, V. (2005) Insights into peptide-based vaccine design for cancer immunotherapy Curr. Med. Chem. 12, 1481-1494
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1481-1494
    • Lazoura, E.1    Apostolopoulos, V.2
  • 11
    • 28344437532 scopus 로고    scopus 로고
    • Stable, soluble, high-affinity, engineered T cell receptors: Novel antibody-like proteins for specific targeting of peptide antigens
    • Boulter, J. M. and Jakobsen, B. K. (2005) Stable, soluble, high-affinity, engineered T cell receptors: Novel antibody-like proteins for specific targeting of peptide antigens Clin. Exp. Immunol. 142, 454-460
    • (2005) Clin. Exp. Immunol. , vol.142 , pp. 454-460
    • Boulter, J.M.1    Jakobsen, B.K.2
  • 12
    • 33749434105 scopus 로고    scopus 로고
    • Engineered T cell receptors and their potential in molecular medicine
    • Miles, J. J., Silins, S. L., and Burrows, S. R. (2006) Engineered T cell receptors and their potential in molecular medicine Curr. Med. Chem. 13, 2725-2736
    • (2006) Curr. Med. Chem. , vol.13 , pp. 2725-2736
    • Miles, J.J.1    Silins, S.L.2    Burrows, S.R.3
  • 13
    • 33747586117 scopus 로고    scopus 로고
    • Making high-affinity T-cell receptors: A new class of targeted therapeutics
    • Ashfield, R. and Jakobsen, B. K. (2006) Making high-affinity T-cell receptors: A new class of targeted therapeutics IDrugs 9, 554-559
    • (2006) IDrugs , vol.9 , pp. 554-559
    • Ashfield, R.1    Jakobsen, B.K.2
  • 14
    • 34548592046 scopus 로고    scopus 로고
    • Display, engineering, and applications of antigen-specific T cell receptors
    • Richman, S. A. and Kranz, D. M. (2007) Display, engineering, and applications of antigen-specific T cell receptors Biomol. Eng. 24, 361-373
    • (2007) Biomol. Eng. , vol.24 , pp. 361-373
    • Richman, S.A.1    Kranz, D.M.2
  • 15
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi, D. N., Ghosh, P., Utz, U., Fan, Q. R., Biddison, W. E., and Wiley, D. C. (1996) Structure of the complex between human T-cell receptor, viral peptide and HLA-A2 Nature 384, 134-141
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 16
    • 0033165928 scopus 로고    scopus 로고
    • Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
    • Ding, Y. H., Baker, B. M., Garboczi, D. N., Biddison, W. E., and Wiley, D. C. (1999) Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical Immunity 11, 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
  • 17
    • 12544253697 scopus 로고    scopus 로고
    • Two different T cell receptors use different thermodynamic strategies to recognize the same peptide/MHC ligand
    • Davis-Harrison, R. L., Armstrong, K. M., and Baker, B. M. (2005) Two different T cell receptors use different thermodynamic strategies to recognize the same peptide/MHC ligand J. Mol. Biol. 346, 533-550
    • (2005) J. Mol. Biol. , vol.346 , pp. 533-550
    • Davis-Harrison, R.L.1    Armstrong, K.M.2    Baker, B.M.3
  • 18
    • 34447299949 scopus 로고    scopus 로고
    • A comprehensive calorimetric investigation of an entropically driven T cell receptor-peptide/major histocompatibility complex interaction
    • Armstrong, K. M. and Baker, B. M. (2007) A comprehensive calorimetric investigation of an entropically driven T cell receptor-peptide/major histocompatibility complex interaction Biophys. J. 93, 597-609
    • (2007) Biophys. J. , vol.93 , pp. 597-609
    • Armstrong, K.M.1    Baker, B.M.2
  • 19
    • 61449234107 scopus 로고    scopus 로고
    • Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC
    • Haidar, J. N., Pierce, B., Yu, Y., Tong, W., Li, M., and Weng, Z. (2009) Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC Proteins 74, 948-960
    • (2009) Proteins , vol.74 , pp. 948-960
    • Haidar, J.N.1    Pierce, B.2    Yu, Y.3    Tong, W.4    Li, M.5    Weng, Z.6
  • 21
    • 0030589221 scopus 로고    scopus 로고
    • Assembly, specific binding, and crystallization of a human TCR-αβ with an antigenic Tax peptide from human T lymphotropic virus type 1 and the class i MHC molecule HLA-A2
    • Garboczi, D. N., Utz, U., Ghosh, P., Seth, A., Kim, J., VanTienhoven, E. A., Biddison, W. E., and Wiley, D. C. (1996) Assembly, specific binding, and crystallization of a human TCR-αβ with an antigenic Tax peptide from human T lymphotropic virus type 1 and the class I MHC molecule HLA-A2 J. Immunol. 157, 5403-5410
    • (1996) J. Immunol. , vol.157 , pp. 5403-5410
    • Garboczi, D.N.1    Utz, U.2    Ghosh, P.3    Seth, A.4    Kim, J.5    Vantienhoven, E.A.6    Biddison, W.E.7    Wiley, D.C.8
  • 22
    • 0026529908 scopus 로고
    • HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides
    • Garboczi, D. N., Hung, D. T., and Wiley, D. C. (1992) HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides Proc. Natl. Acad. Sci. U.S.A. 89, 3429-3433
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 3429-3433
    • Garboczi, D.N.1    Hung, D.T.2    Wiley, D.C.3
  • 23
    • 0033955735 scopus 로고    scopus 로고
    • Advances in surface plasmon resonance biosensor analysis
    • Rich, R. L. and Myszka, D. G. (2000) Advances in surface plasmon resonance biosensor analysis Curr. Opin. Biotechnol. 11, 54-61
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 54-61
    • Rich, R.L.1    Myszka, D.G.2
  • 24
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for binding energy hot spots in protein-protein complexes
    • Kortemme, T. and Baker, D. (2002) A simple physical model for binding energy hot spots in protein-protein complexes Proc. Natl. Acad. Sci. U.S.A. 99, 14116-14121
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14116-14121
    • Kortemme, T.1    Baker, D.2
  • 27
    • 0031552370 scopus 로고    scopus 로고
    • Determination of atomic desolvation energies from the structures of crystallized proteins
    • Zhang, C., Vasmatzis, G., Cornette, J. L., and DeLisi, C. (1997) Determination of atomic desolvation energies from the structures of crystallized proteins J. Mol. Biol. 267, 707-726
    • (1997) J. Mol. Biol. , vol.267 , pp. 707-726
    • Zhang, C.1    Vasmatzis, G.2    Cornette, J.L.3    Delisi, C.4
  • 29
    • 54249137135 scopus 로고    scopus 로고
    • Computational redesign of a protein-protein interface for high affinity and binding specificity using modular architecture and naturally occurring template fragments
    • Potapov, V., Reichmann, D., Abramovich, R., Filchtinski, D., Zohar, N., Ben Halevy, D., Edelman, M., Sobolev, V., and Schreiber, G. (2008) Computational redesign of a protein-protein interface for high affinity and binding specificity using modular architecture and naturally occurring template fragments J. Mol. Biol. 384, 109-119
    • (2008) J. Mol. Biol. , vol.384 , pp. 109-119
    • Potapov, V.1    Reichmann, D.2    Abramovich, R.3    Filchtinski, D.4    Zohar, N.5    Ben Halevy, D.6    Edelman, M.7    Sobolev, V.8    Schreiber, G.9
  • 30
    • 0036682133 scopus 로고    scopus 로고
    • Two-step binding mechanism for T-cell receptor recognition of peptide MHC
    • Wu, L. C., Tuot, D. S., Lyons, D. S., Garcia, K. C., and Davis, M. M. (2002) Two-step binding mechanism for T-cell receptor recognition of peptide MHC Nature 418, 552-556
    • (2002) Nature , vol.418 , pp. 552-556
    • Wu, L.C.1    Tuot, D.S.2    Lyons, D.S.3    Garcia, K.C.4    Davis, M.M.5
  • 31
    • 33847021917 scopus 로고    scopus 로고
    • T cell receptor binding transition states and recognition of peptide/MHC
    • Davis-Harrison, R. L., Insaidoo, F. K., and Baker, B. M. (2007) T cell receptor binding transition states and recognition of peptide/MHC Biochemistry 46, 1840-1850
    • (2007) Biochemistry , vol.46 , pp. 1840-1850
    • Davis-Harrison, R.L.1    Insaidoo, F.K.2    Baker, B.M.3
  • 33
    • 58149280299 scopus 로고    scopus 로고
    • T-cell receptor binding affinities and kinetics: Impact on T-cell activity and specificity
    • Stone, J. D., Chervin, A. S., and Kranz, D. M. (2009) T-cell receptor binding affinities and kinetics: Impact on T-cell activity and specificity Immunology 126, 165-176
    • (2009) Immunology , vol.126 , pp. 165-176
    • Stone, J.D.1    Chervin, A.S.2    Kranz, D.M.3
  • 34
    • 0033524394 scopus 로고    scopus 로고
    • Biophysical characterization of the interaction of the β-lactamase TEM-1 with its protein inhibitor BLIP
    • Albeck, S. and Schreiber, G. (1999) Biophysical characterization of the interaction of the β-lactamase TEM-1 with its protein inhibitor BLIP Biochemistry 38, 11-21
    • (1999) Biochemistry , vol.38 , pp. 11-21
    • Albeck, S.1    Schreiber, G.2
  • 35
    • 47649130715 scopus 로고    scopus 로고
    • Thermodynamics of T-cell receptor-peptide/MHC interactions: Progress and opportunities
    • Armstrong, K. M., Insaidoo, F. K., and Baker, B. M. (2008) Thermodynamics of T-cell receptor-peptide/MHC interactions: Progress and opportunities J. Mol. Recognit. 21, 275-287
    • (2008) J. Mol. Recognit. , vol.21 , pp. 275-287
    • Armstrong, K.M.1    Insaidoo, F.K.2    Baker, B.M.3
  • 37
    • 30044449525 scopus 로고    scopus 로고
    • Class II-restricted T cell receptor engineered in vitro for higher affinity retains peptide specificity and function
    • Weber, K. S., Donermeyer, D. L., Allen, P. M., and Kranz, D. M. (2005) Class II-restricted T cell receptor engineered in vitro for higher affinity retains peptide specificity and function Proc. Natl. Acad. Sci. U.S.A. 102, 19033-19038
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 19033-19038
    • Weber, K.S.1    Donermeyer, D.L.2    Allen, P.M.3    Kranz, D.M.4
  • 39
    • 54049111388 scopus 로고    scopus 로고
    • Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes
    • Armstrong, K. M., Piepenbrink, K. H., and Baker, B. M. (2008) Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes Biochem. J. 415, 183-196
    • (2008) Biochem. J. , vol.415 , pp. 183-196
    • Armstrong, K.M.1    Piepenbrink, K.H.2    Baker, B.M.3
  • 40
    • 2942659074 scopus 로고    scopus 로고
    • T cell receptor-ligand interactions: A conformational preequilibrium or an induced fit
    • Gakamsky, D. M., Luescher, I. F., and Pecht, I. (2004) T cell receptor-ligand interactions: A conformational preequilibrium or an induced fit Proc. Natl. Acad. Sci. U.S.A. 101, 9063-9066
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9063-9066
    • Gakamsky, D.M.1    Luescher, I.F.2    Pecht, I.3
  • 41
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Schreiber, G. (2002) Kinetic studies of protein-protein interactions Curr. Opin. Struct. Biol. 12, 41-47
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 42
    • 34447101383 scopus 로고    scopus 로고
    • On the dynamic nature of the transition state for protein-protein association as determined by double-mutant cycle analysis and simulation
    • Harel, M., Cohen, M., and Schreiber, G. (2007) On the dynamic nature of the transition state for protein-protein association as determined by double-mutant cycle analysis and simulation J. Mol. Biol. 371, 180-196
    • (2007) J. Mol. Biol. , vol.371 , pp. 180-196
    • Harel, M.1    Cohen, M.2    Schreiber, G.3
  • 43
    • 0035917323 scopus 로고    scopus 로고
    • Experimental assignment of the structure of the transition state for the association of barnase and barstar
    • Frisch, C., Fersht, A. R., and Schreiber, G. (2001) Experimental assignment of the structure of the transition state for the association of barnase and barstar J. Mol. Biol. 308, 69-77
    • (2001) J. Mol. Biol. , vol.308 , pp. 69-77
    • Frisch, C.1    Fersht, A.R.2    Schreiber, G.3
  • 47
    • 31344460657 scopus 로고    scopus 로고
    • Context-dependent mutations predominate in an engineered high-affinity single chain antibody fragment
    • Midelfort, K. S. and Wittrup, K. D. (2006) Context-dependent mutations predominate in an engineered high-affinity single chain antibody fragment Protein Sci. 15, 324-334
    • (2006) Protein Sci. , vol.15 , pp. 324-334
    • Midelfort, K.S.1    Wittrup, K.D.2


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