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Volumn 352, Issue 3, 2005, Pages 656-671

The kinetic basis for dual recognition in colicin endonuclease-immunity protein complexes

Author keywords

Antibody; ITC; Kinetics; Stopped flow; T cell receptor

Indexed keywords

COLICIN; DEOXYRIBONUCLEASE; ENDONUCLEASE; T LYMPHOCYTE RECEPTOR;

EID: 24044523202     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.07.035     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 0036589253 scopus 로고    scopus 로고
    • Killing of E. coli cells by e group nuclease colicins
    • R. James, C.N. Penfold, G.R. Moore, and C. Kleanthous Killing of E. coli cells by E group nuclease colicins Biochimie 84 2002 381 389
    • (2002) Biochimie , vol.84 , pp. 381-389
    • James, R.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4
  • 3
    • 0031939176 scopus 로고    scopus 로고
    • Immunity proteins and their specificity for endonuclease colicins: Telling right from wrong in protein-protein recognition
    • C. Kleanthous, A.M. Hemmings, G.R. Moore, and R. James Immunity proteins and their specificity for endonuclease colicins: telling right from wrong in protein-protein recognition Mol. Microbiol. 28 1998 227 233
    • (1998) Mol. Microbiol. , vol.28 , pp. 227-233
    • Kleanthous, C.1    Hemmings, A.M.2    Moore, G.R.3    James, R.4
  • 4
    • 0001781875 scopus 로고    scopus 로고
    • Nuclease inhibitors
    • C. Kleanthous Oxford University Press Oxford
    • C. Kleanthous, and A.J. Pommer Nuclease inhibitors C. Kleanthous Protein-Protein Recognition 2000 Oxford University Press Oxford 280 311
    • (2000) Protein-Protein Recognition , pp. 280-311
    • Kleanthous, C.1    Pommer, A.J.2
  • 5
    • 0035478958 scopus 로고    scopus 로고
    • Immunity proteins: Enzyme inhibitors that avoid the active site
    • C. Kleanthous, and D. Walker Immunity proteins: enzyme inhibitors that avoid the active site Trends Biochem. Sci. 26 2001 624 631
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 624-631
    • Kleanthous, C.1    Walker, D.2
  • 6
    • 0028866770 scopus 로고
    • Protein-protein interactions in colicin E9 DNase - Immunity protein complexes. 1. Diffusion-controlled association and femtomolar binding for the cognate complex
    • R. Wallis, G.R. Moore, R. James, and C. Kleanthous Protein-protein interactions in colicin E9 DNase - immunity protein complexes. 1. Diffusion-controlled association and femtomolar binding for the cognate complex Biochemistry 34 1995 13743 13750
    • (1995) Biochemistry , vol.34 , pp. 13743-13750
    • Wallis, R.1    Moore, G.R.2    James, R.3    Kleanthous, C.4
  • 7
    • 0028886403 scopus 로고
    • Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 2. Cognate and non-cognate interactions that span the millimolar to femtomolar affinity range
    • R. Wallis, K.-Y. Leung, A.J. Pommer, H. Videler, G.R. Moore, R. James, and C. Kleanthous Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 2. Cognate and non-cognate interactions that span the millimolar to femtomolar affinity range Biochemistry 34 1995 13751 13759
    • (1995) Biochemistry , vol.34 , pp. 13751-13759
    • Wallis, R.1    Leung, K.-Y.2    Pommer, A.J.3    Videler, H.4    Moore, G.R.5    James, R.6    Kleanthous, C.7
  • 8
    • 1542358785 scopus 로고    scopus 로고
    • Highly discriminating protein-protein interaction specificities in the context of a conserved binding energy hotspot
    • W. Li, A.H. Keeble, C. Giffard, R. James, G.R. Moore, and C. Kleanthous Highly discriminating protein-protein interaction specificities in the context of a conserved binding energy hotspot J. Mol. Biol. 337 2004 743 759
    • (2004) J. Mol. Biol. , vol.337 , pp. 743-759
    • Li, W.1    Keeble, A.H.2    Giffard, C.3    James, R.4    Moore, G.R.5    Kleanthous, C.6
  • 9
    • 0032566286 scopus 로고    scopus 로고
    • Dual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactions
    • W. Li, S.J. Hamill, A.M. Hemmings, G.R. Moore, R. James, and C. Kleanthous Dual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactions Biochemistry 37 1998 11771 11779
    • (1998) Biochemistry , vol.37 , pp. 11771-11779
    • Li, W.1    Hamill, S.J.2    Hemmings, A.M.3    Moore, G.R.4    James, R.5    Kleanthous, C.6
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 14
    • 0036682133 scopus 로고    scopus 로고
    • Two-step binding mechanism for T-cell receptor recognition of peptide MHC
    • L.C. Wu, D.S. Tuot, D.S. Lyons, K.C. Garcia, and M.M. Davis Two-step binding mechanism for T-cell receptor recognition of peptide MHC Nature 418 2002 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
  • 17
    • 0032169937 scopus 로고    scopus 로고
    • Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli
    • A.J. Pommer, R. Wallis, G.R. Moore, R. James, and C. Kleanthous Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli Biochem. J. 334 1998 387 392
    • (1998) Biochem. J. , vol.334 , pp. 387-392
    • Pommer, A.J.1    Wallis, R.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 18
    • 0026724613 scopus 로고
    • In vivo and in vitro characterization of overproduced colicin E9 immunity protein
    • R. Wallis, A. Reilly, A. Rowe, G.R. Moore, R. James, and C. Kleanthous In vivo and in vitro characterization of overproduced colicin E9 immunity protein Eur. J. Biochem. 207 1992 687 695
    • (1992) Eur. J. Biochem. , vol.207 , pp. 687-695
    • Wallis, R.1    Reilly, A.2    Rowe, A.3    Moore, G.R.4    James, R.5    Kleanthous, C.6
  • 19
    • 0032512424 scopus 로고    scopus 로고
    • Specificity in protein-protein recognition: Conserved Im9 residues are the major determinants of stability in the colicin E9 DNase-Im9 complex
    • R. Wallis, K.-Y. Leung, M.J. Osborne, R. James, G.R. Moore, and C. Kleanthous Specificity in protein-protein recognition: conserved Im9 residues are the major determinants of stability in the colicin E9 DNase-Im9 complex Biochemistry 37 1998 476 485
    • (1998) Biochemistry , vol.37 , pp. 476-485
    • Wallis, R.1    Leung, K.-Y.2    Osborne, M.J.3    James, R.4    Moore, G.R.5    Kleanthous, C.6
  • 21
    • 0034051071 scopus 로고    scopus 로고
    • Slow conformational dynamics of an endonuclease persist in its complex with its natural protein inhibitor
    • S.B. Whittaker, M. Czisch, R. Wechselberger, R. Kaptein, A.M. Hemmings, and R. James Slow conformational dynamics of an endonuclease persist in its complex with its natural protein inhibitor Protein Sci. 9 2000 713 720
    • (2000) Protein Sci. , vol.9 , pp. 713-720
    • Whittaker, S.B.1    Czisch, M.2    Wechselberger, R.3    Kaptein, R.4    Hemmings, A.M.5    James, R.6
  • 24
    • 24044468582 scopus 로고    scopus 로고
    • Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: Analysis of stopped-flow kinetic experiments
    • R. Galletto, M.J. Jezewska, and W. Bujalowski Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: analysis of stopped-flow kinetic experiments Cell Biochem. Biophys. 42 2005 121 144
    • (2005) Cell Biochem. Biophys. , vol.42 , pp. 121-144
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 26
    • 0037072261 scopus 로고    scopus 로고
    • Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9
    • A.H. Keeble, A.M. Hemmings, R. James, G.R. Moore, and C. Kleanthous Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9 Biochemistry 41 2002 10234 10244
    • (2002) Biochemistry , vol.41 , pp. 10234-10244
    • Keeble, A.H.1    Hemmings, A.M.2    James, R.3    Moore, G.R.4    Kleanthous, C.5
  • 27
    • 1342302339 scopus 로고    scopus 로고
    • Conformational changes associated with protein-protein interactions
    • C.S. Goh, D. Milburn, and M. Gerstein Conformational changes associated with protein-protein interactions Curr. Opin. Struct. Biol. 14 2004 104 109
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 104-109
    • Goh, C.S.1    Milburn, D.2    Gerstein, M.3
  • 28
    • 0032127769 scopus 로고    scopus 로고
    • A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity
    • C.A. Dennis, H. Videler, R.A. Pauptit, R. Wallis, R. James, G.R. Moore, and C. Kleanthous A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity Biochem. J. 333 1998 183 191
    • (1998) Biochem. J. , vol.333 , pp. 183-191
    • Dennis, C.A.1    Videler, H.2    Pauptit, R.A.3    Wallis, R.4    James, R.5    Moore, G.R.6    Kleanthous, C.7
  • 29
    • 0002347541 scopus 로고    scopus 로고
    • The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein
    • T.P. Ko, C.C. Liao, W.Y. Ku, K.F. Chak, and H.S. Yuan The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein Structure 7 1999 97 102
    • (1999) Structure , vol.7 , pp. 97-102
    • Ko, T.P.1    Liao, C.C.2    Ku, W.Y.3    Chak, K.F.4    Yuan, H.S.5
  • 30
    • 0036440979 scopus 로고    scopus 로고
    • The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases
    • Y.S. Cheng, K.C. Hsia, L.G. Doudeva, K.F. Chak, and H.S. Yuan The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases J. Mol. Biol. 324 2002 227 236
    • (2002) J. Mol. Biol. , vol.324 , pp. 227-236
    • Cheng, Y.S.1    Hsia, K.C.2    Doudeva, L.G.3    Chak, K.F.4    Yuan, H.S.5
  • 33
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: Analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • G. Schreiber, and A.R. Fersht Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles J. Mol. Biol. 248 1995 478 486
    • (1995) J. Mol. Biol. , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 34
    • 0033587484 scopus 로고    scopus 로고
    • Superadditive and subadditive effects of "hot spot" mutations within the interfaces of placental ribonuclease inhibitor with angiogenin and ribonuclease a
    • C.Z. Chen, and R. Shapiro Superadditive and subadditive effects of "hot spot" mutations within the interfaces of placental ribonuclease inhibitor with angiogenin and ribonuclease A Biochemistry 38 1999 9273 9285
    • (1999) Biochemistry , vol.38 , pp. 9273-9285
    • Chen, C.Z.1    Shapiro, R.2
  • 35
    • 0034283147 scopus 로고    scopus 로고
    • Specificity in protein-protein interactions: The structural basis for dual recognition in endonuclease colicin-immunity protein complexes
    • U.C. Kühlmann, A.J. Pommer, G.R. Moore, R. James, and C. Kleanthous Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes J. Mol. Biol. 301 2000 1163 1178
    • (2000) J. Mol. Biol. , vol.301 , pp. 1163-1178
    • Kühlmann, U.C.1    Pommer, A.J.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 36
    • 11844273937 scopus 로고    scopus 로고
    • Directed evolution of protein inhibitors of DNA-nucleases by in vitro compartmentalization (IVC) and nano-droplet delivery
    • K. Bernath, S. Magdassi, and D.S. Tawfik Directed evolution of protein inhibitors of DNA-nucleases by in vitro compartmentalization (IVC) and nano-droplet delivery J. Mol. Biol. 345 2005 1015 1026
    • (2005) J. Mol. Biol. , vol.345 , pp. 1015-1026
    • Bernath, K.1    Magdassi, S.2    Tawfik, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.