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Volumn 365, Issue 3, 2007, Pages 663-679

Binding Hot Spots in the TEM1-BLIP Interface in Light of its Modular Architecture

Author keywords

energetics; hot spots; protein protein interaction; structure function; X ray

Indexed keywords

AMINO ACID; BETA LACTAMASE; PROTEIN;

EID: 33845661569     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.09.076     Document Type: Article
Times cited : (81)

References (42)
  • 1
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., and Wells J.A. A hot spot of binding energy in a hormone-receptor interface. Science 267 (1995) 383-386
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 2
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan A.A., and Thorn K.S. 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
  • 3
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren I.M., and Thornton J.M. Structural characterisation and functional significance of transient protein-protein interactions. J. Mol. Biol. 325 (2003) 991-1018
    • (2003) J. Mol. Biol. , vol.325 , pp. 991-1018
    • Nooren, I.M.1    Thornton, J.M.2
  • 4
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations
    • Guerois R., Nielsen J.E., and Serrano L. 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
  • 5
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for binding energy hot spots in protein-protein complexes
    • Kortemme T., and Baker D. 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
  • 6
    • 0030322783 scopus 로고    scopus 로고
    • Double-mutant cycles: a powerful tool for analyzing protein structure and function
    • Horovitz A. Double-mutant cycles: a powerful tool for analyzing protein structure and function. Fold. Des. 1 (1996) R121-R126
    • (1996) Fold. Des. , vol.1
    • Horovitz, A.1
  • 7
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., Chothia C., and Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285 (1999) 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 8
    • 0034213559 scopus 로고    scopus 로고
    • Conservation of polar residues as hot spots at protein interfaces
    • Hu Z., Ma B., Wolfson H., and Nussinov R. Conservation of polar residues as hot spots at protein interfaces. Proteins: Struct. Funct. Genet. 39 (2000) 331-342
    • (2000) Proteins: Struct. Funct. Genet. , vol.39 , pp. 331-342
    • Hu, Z.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 9
    • 14144256681 scopus 로고    scopus 로고
    • Energy functions for protein design: adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity
    • Pokala N., and Handel T.M. Energy functions for protein design: adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity. J. Mol. Biol. 347 (2005) 203-227
    • (2005) J. Mol. Biol. , vol.347 , pp. 203-227
    • Pokala, N.1    Handel, T.M.2
  • 11
    • 0001289724 scopus 로고
    • Einflus der configuration auf die wirkung derenzyme
    • Fisher E. Einflus der configuration auf die wirkung derenzyme. Ber. Dt. Chem. Ges 27 (1894) 751
    • (1894) Ber. Dt. Chem. Ges , vol.27 , pp. 751
    • Fisher, E.1
  • 12
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland D.E. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl Acad. Sci. USA 44 (1958) 98-104
    • (1958) Proc. Natl Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 13
    • 0036093538 scopus 로고    scopus 로고
    • Analysis of homodimeric protein interfaces by graph-spectral methods
    • Brinda K.V., Kannan N., and Vishveshwara S. Analysis of homodimeric protein interfaces by graph-spectral methods. Protein Eng. 15 (2002) 265-277
    • (2002) Protein Eng. , vol.15 , pp. 265-277
    • Brinda, K.V.1    Kannan, N.2    Vishveshwara, S.3
  • 14
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar I., Atilgan A.R., and Erman B. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Fold. Des. 2 (1997) 173-181
    • (1997) Fold. Des. , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 15
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues form a critical contact network in a protein folding transition state
    • Vendruscolo M., Paci E., Dobson C.M., and Karplus M. Three key residues form a critical contact network in a protein folding transition state. Nature 409 (2001) 641-645
    • (2001) Nature , vol.409 , pp. 641-645
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 18
    • 4644290827 scopus 로고    scopus 로고
    • Using networks to identify fine structural differences between functionally distinct protein states
    • Swint-Kruse L. Using networks to identify fine structural differences between functionally distinct protein states. Biochemistry 43 (2004) 10886-10895
    • (2004) Biochemistry , vol.43 , pp. 10886-10895
    • Swint-Kruse, L.1
  • 19
    • 0034607551 scopus 로고    scopus 로고
    • Evaluation of direct and cooperative contributions towards the strength of buried hydrogen bonds and salt bridges
    • Albeck S., Unger R., and Schreiber G. 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
  • 20
    • 0030795295 scopus 로고    scopus 로고
    • Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors
    • Schuck P. Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors. Curr. Opin. Biotechnol. 8 (1997) 498-502
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 498-502
    • Schuck, P.1
  • 21
    • 0344177897 scopus 로고    scopus 로고
    • Present and future of surface plasmon resonance biosensors
    • Homola J. Present and future of surface plasmon resonance biosensors. Anal. Bioanal. Chem. 377 (2003) 528-539
    • (2003) Anal. Bioanal. Chem. , vol.377 , pp. 528-539
    • Homola, J.1
  • 22
    • 0034581194 scopus 로고    scopus 로고
    • Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE
    • Myszka D.G. Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE. Methods Enzymol. 323 (2000) 325-340
    • (2000) Methods Enzymol. , vol.323 , pp. 325-340
    • Myszka, D.G.1
  • 23
    • 0033923367 scopus 로고    scopus 로고
    • Rational design of faster associating and tighter binding protein complexes
    • Selzer T., Albeck S., and Schreiber G. Rational design of faster associating and tighter binding protein complexes. Nature Struct. Biol. 7 (2000) 537-541
    • (2000) Nature Struct. Biol. , vol.7 , pp. 537-541
    • Selzer, T.1    Albeck, S.2    Schreiber, G.3
  • 24
    • 5644266081 scopus 로고    scopus 로고
    • Dissecting the protein-protein interface between beta-lactamase inhibitory protein and class A beta-lactamases
    • Zhang Z., and Palzkill T. Dissecting the protein-protein interface between beta-lactamase inhibitory protein and class A beta-lactamases. J. Biol. Chem. 279 (2004) 42860-42866
    • (2004) J. Biol. Chem. , vol.279 , pp. 42860-42866
    • Zhang, Z.1    Palzkill, T.2
  • 25
    • 0033524394 scopus 로고    scopus 로고
    • Biophysical characterization of the interaction of the beta-lactamase TEM-1 with its protein inhibitor BLIP
    • Albeck S., and Schreiber G. Biophysical characterization of the interaction of the beta-lactamase TEM-1 with its protein inhibitor BLIP. Biochemistry 38 (1999) 11-21
    • (1999) Biochemistry , vol.38 , pp. 11-21
    • Albeck, S.1    Schreiber, G.2
  • 27
    • 33748753961 scopus 로고    scopus 로고
    • Structural and computational characterization of the SHV-1 beta -lactamase/beta -lactamase inhibitor protein(BLIP) interface
    • Reynolds K.A., Thomson J.M., Corbett K.D., Bethel C.R., Berger J.M., Kirsch J.F., et al. Structural and computational characterization of the SHV-1 beta -lactamase/beta -lactamase inhibitor protein(BLIP) interface. J. Biol. Chem. 281 (2006) 26745-26753
    • (2006) J. Biol. Chem. , vol.281 , pp. 26745-26753
    • Reynolds, K.A.1    Thomson, J.M.2    Corbett, K.D.3    Bethel, C.R.4    Berger, J.M.5    Kirsch, J.F.6
  • 29
    • 1842788912 scopus 로고    scopus 로고
    • Importance of solvent accessibility and contact surfaces in modeling side-chain conformations in proteins
    • Eyal E., Najmanovich R., McConkey B.J., Edelman M., and Sobolev V. Importance of solvent accessibility and contact surfaces in modeling side-chain conformations in proteins. J. Comput. Chem. 25 (2004) 712-724
    • (2004) J. Comput. Chem. , vol.25 , pp. 712-724
    • Eyal, E.1    Najmanovich, R.2    McConkey, B.J.3    Edelman, M.4    Sobolev, V.5
  • 30
    • 0037035548 scopus 로고    scopus 로고
    • Double mutant studies identify electrostatic interactions that are important for docking cytochrome c2 onto the bacterial reaction center
    • Tetreault M., Cusanovich M., Meyer T., Axelrod H., and Okamura M.Y. Double mutant studies identify electrostatic interactions that are important for docking cytochrome c2 onto the bacterial reaction center. Biochemistry 41 (2002) 5807-5815
    • (2002) Biochemistry , vol.41 , pp. 5807-5815
    • Tetreault, M.1    Cusanovich, M.2    Meyer, T.3    Axelrod, H.4    Okamura, M.Y.5
  • 31
    • 0034804715 scopus 로고    scopus 로고
    • Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase
    • Lim D., Park H.U., De Castro L., Kang S.G., Lee H.S., Jensen S., et al. Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase. Nature Struct. Biol. 8 (2001) 848-852
    • (2001) Nature Struct. Biol. , vol.8 , pp. 848-852
    • Lim, D.1    Park, H.U.2    De Castro, L.3    Kang, S.G.4    Lee, H.S.5    Jensen, S.6
  • 32
    • 0034746243 scopus 로고    scopus 로고
    • Construction and analysis of ss-lactamase-inhibitory protein (BLIP) non-producer mutants of Streptomyces clavuligerus
    • Thai W., Paradkar A.S., and Jensen S.E. Construction and analysis of ss-lactamase-inhibitory protein (BLIP) non-producer mutants of Streptomyces clavuligerus. Microbiology 147 (2001) 325-335
    • (2001) Microbiology , vol.147 , pp. 325-335
    • Thai, W.1    Paradkar, A.S.2    Jensen, S.E.3
  • 33
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T.A., Roberts J.D., and Zakour R.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154 (1987) 367-382
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 35
    • 33745966693 scopus 로고    scopus 로고
    • Variations in the unstructured C-terminal tail of interferons contribute to differential receptor binding and biological activity
    • Slutzki M., Jaitin D.A., Ben Yehezkel T., and Schreiber G. Variations in the unstructured C-terminal tail of interferons contribute to differential receptor binding and biological activity. J. Mol. Biol. 360 (2006) 1019-1030
    • (2006) J. Mol. Biol. , vol.360 , pp. 1019-1030
    • Slutzki, M.1    Jaitin, D.A.2    Ben Yehezkel, T.3    Schreiber, G.4
  • 36
    • 0021504608 scopus 로고
    • The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
    • Carter P.J., Winter G., Wilkinson A.J., and Fersht A.R. The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell 38 (1984) 835-840
    • (1984) Cell , vol.38 , pp. 835-840
    • Carter, P.J.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 37
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word J.M., Lovell S.C., Richardson J.S., and Richardson D.C. Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol. 285 (1999) 1735-1747
    • (1999) J. Mol. Biol. , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 38
    • 0033613812 scopus 로고    scopus 로고
    • Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms
    • Word J.M., Lovell S.C., LaBean T.H., Taylor H.C., Zalis M.E., Presley B.K., et al. Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms. J. Mol. Biol. 285 (1999) 1711-1733
    • (1999) J. Mol. Biol. , vol.285 , pp. 1711-1733
    • Word, J.M.1    Lovell, S.C.2    LaBean, T.H.3    Taylor, H.C.4    Zalis, M.E.5    Presley, B.K.6
  • 39
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly M.L. Solvent-accessible surfaces of proteins and nucleic acids. Science 221 (1983) 709-713
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 40
    • 0042622395 scopus 로고    scopus 로고
    • NCI: a server to identify non-canonical interactions in protein structures
    • Babu M.M. NCI: a server to identify non-canonical interactions in protein structures. Nucl. Acids Res. 31 (2003) 3345-3348
    • (2003) Nucl. Acids Res. , vol.31 , pp. 3345-3348
    • Babu, M.M.1
  • 41
    • 0028287903 scopus 로고
    • Structural and kinetic characterization of a beta-lactamase-inhibitor protein
    • Strynadka N.C., Jensen S.E., Johns K., Blanchard H., Page M., Matagne A., et al. Structural and kinetic characterization of a beta-lactamase-inhibitor protein. Nature 368 (1994) 657-660
    • (1994) Nature , vol.368 , pp. 657-660
    • Strynadka, N.C.1    Jensen, S.E.2    Johns, K.3    Blanchard, H.4    Page, M.5    Matagne, A.6
  • 42
    • 3242879771 scopus 로고    scopus 로고
    • Computational alanine scanning of protein-protein interfaces
    • Kortemme T., Kim D.E., and Baker D. Computational alanine scanning of protein-protein interfaces. Sci. STKE 2004 (2004) 12
    • (2004) Sci. STKE , vol.2004 , pp. 12
    • Kortemme, T.1    Kim, D.E.2    Baker, D.3


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