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Volumn 340, Issue 2, 2004, Pages 253-261

Computational and experimental probes of symmetry mismatches in the Arc repressor-DNA complex

Author keywords

continuum electrostatics; DNA binding protein; EMSA, electrophoretic mobility shift assay; protein DNA interactions; scArc, single chain Arc repressor

Indexed keywords

ARGININE; DIMER; DNA; DNA BINDING PROTEIN; GLUTAMINE; REPRESSOR PROTEIN; REPRESSOR PROTEIN ARC; UNCLASSIFIED DRUG;

EID: 2942601118     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.026     Document Type: Article
Times cited : (4)

References (21)
  • 1
    • 0028177303 scopus 로고
    • DNA recognition by beta-sheets in the Arc repressor-operator crystal structure
    • Raumann B.E., Rould M.A., Pabo C.O., Sauer R.T. DNA recognition by beta-sheets in the Arc repressor-operator crystal structure. Nature. 367:1994;754-757
    • (1994) Nature , vol.367 , pp. 754-757
    • Raumann, B.E.1    Rould, M.A.2    Pabo, C.O.3    Sauer, R.T.4
  • 2
    • 0026641755 scopus 로고
    • Crystal structure of the Met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by b-strands
    • Somers W.S., Phillips E.V. Crystal structure of the Met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by b-strands. Nature. 359:1992;387-393
    • (1992) Nature , vol.359 , pp. 387-393
    • Somers, W.S.1    Phillips, E.V.2
  • 3
    • 0028403242 scopus 로고
    • Scanning mutagenesis of the Arc repressor as a functional probe of operator recognition
    • Brown B.M., Milla M.E., Smith T.L., Sauer R.T. Scanning mutagenesis of the Arc repressor as a functional probe of operator recognition. Nature Struct. Biol. 1:1994;164-168
    • (1994) Nature Struct. Biol. , vol.1 , pp. 164-168
    • Brown, B.M.1    Milla, M.E.2    Smith, T.L.3    Sauer, R.T.4
  • 4
    • 0001586362 scopus 로고
    • Identifying determinants of folding and activity for a protein of unknown structure
    • Bowie J.U., Sauer R.T. Identifying determinants of folding and activity for a protein of unknown structure. Proc. Natl Acad. Sci. USA. 86:1989;2152-2156
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 2152-2156
    • Bowie, J.U.1    Sauer, R.T.2
  • 5
    • 0024977947 scopus 로고
    • Sequence-specific binding of Arc repressor to DNA. Effects of operator mutations and modifications
    • Vershon A.K., Kelley R.D., Sauer R.T. Sequence-specific binding of Arc repressor to DNA. Effects of operator mutations and modifications. J. Biol. Chem. 264:1989;3267-3273
    • (1989) J. Biol. Chem. , vol.264 , pp. 3267-3273
    • Vershon, A.K.1    Kelley, R.D.2    Sauer, R.T.3
  • 6
    • 0029671279 scopus 로고    scopus 로고
    • Covalent attachment of Arc repressor subunits by a peptide linker enhances affinity for operator DNA
    • Robinson C.R., Sauer R.T. Covalent attachment of Arc repressor subunits by a peptide linker enhances affinity for operator DNA. Biochemistry. 35:1996;109-116
    • (1996) Biochemistry , vol.35 , pp. 109-116
    • Robinson, C.R.1    Sauer, R.T.2
  • 7
    • 0031165571 scopus 로고    scopus 로고
    • Optimization of electrostatic binding free energy
    • Lee L.P., Tidor B. Optimization of electrostatic binding free energy. J. Chem. Phys. 106:1997;8681-8690
    • (1997) J. Chem. Phys. , vol.106 , pp. 8681-8690
    • Lee, L.P.1    Tidor, B.2
  • 8
  • 9
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution: Method and error assessment
    • Gilson M.K., Sharp K.A., Honig B.H. Calculating the electrostatic potential of molecules in solution: method and error assessment. J. Comput. Chem. 9:1988;327-335
    • (1988) J. Comput. Chem. , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.H.3
  • 10
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis
    • Gilson M.K., Honig B.H. Calculation of the total electrostatic energy of a macromolecular system: solvation energies, binding energies, and conformational analysis. Proteins Struct. Funct. Genet. 4:1988;7-18
    • (1988) Proteins Struct. Funct. Genet. , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.H.2
  • 11
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and applications
    • Sharp K.A., Honig B. Electrostatic interactions in macromolecules: theory and applications. Annu. Rev. Biophys. Biophys. Chem. 19:1990;301-332
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 12
    • 0032789936 scopus 로고    scopus 로고
    • Electrostatic interactions in the GCN4 leucine zipper: Substantial contributions arise from intramolecular interactions enhanced on binding
    • Hendsch Z.S., Tidor B. Electrostatic interactions in the GCN4 leucine zipper: substantial contributions arise from intramolecular interactions enhanced on binding. Protein Sci. 8:1999;1381-1392
    • (1999) Protein Sci. , vol.8 , pp. 1381-1392
    • Hendsch, Z.S.1    Tidor, B.2
  • 13
    • 0031891022 scopus 로고    scopus 로고
    • Computation of electrostatic complements to proteins: A case of charge stabilized binding
    • Chong L.T., Dempster S.E., Hendsch Z.S., Lee L.P., Tidor B. Computation of electrostatic complements to proteins: a case of charge stabilized binding. Protein Sci. 7:1998;206-210
    • (1998) Protein Sci. , vol.7 , pp. 206-210
    • Chong, L.T.1    Dempster, S.E.2    Hendsch, Z.S.3    Lee, L.P.4    Tidor, B.5
  • 14
    • 21944443282 scopus 로고    scopus 로고
    • Optimizing electrostatic affinity in ligand-receptor binding: Theory, computation, and ligand properties
    • Kangas E., Tidor B. Optimizing electrostatic affinity in ligand-receptor binding: theory, computation, and ligand properties. J. Chem. Phys. 109:1998;7522-7545
    • (1998) J. Chem. Phys. , vol.109 , pp. 7522-7545
    • Kangas, E.1    Tidor, B.2
  • 15
    • 0023660382 scopus 로고
    • Interaction of the bacteriophage P22 Arc repressor with operator DNA
    • Vershon A.K., Liao S.M., McClure W.R., Sauer R.T. Interaction of the bacteriophage P22 Arc repressor with operator DNA. J. Mol. Biol. 195:1987;323-331
    • (1987) J. Mol. Biol. , vol.195 , pp. 323-331
    • Vershon, A.K.1    Liao, S.M.2    McClure, W.R.3    Sauer, R.T.4
  • 17
    • 0024250301 scopus 로고
    • Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison
    • Brünger A.T., Karplus M. Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. Proteins: Struct. Funct. Genet. 4:1988;148-156
    • (1988) Proteins: Struct. Funct. Genet. , vol.4 , pp. 148-156
    • Brünger, A.T.1    Karplus, M.2
  • 18
    • 6344260593 scopus 로고
    • An all-atom empirical energy function for the simulation of nucleic-acids
    • Mackerell A.D., Wiorkiewiczkuczera J., Karplus M. An all-atom empirical energy function for the simulation of nucleic-acids. J. Am. Chem. Soc. 117:1995;11946-11975
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11946-11975
    • MacKerell, A.D.1    Wiorkiewiczkuczera, J.2    Karplus, M.3
  • 19
    • 0023280069 scopus 로고
    • Calculation of electrostatic potentials in an enzyme active site
    • Gilson M.K., Honig B.H. Calculation of electrostatic potentials in an enzyme active site. Nature. 330:1987;84-86
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.K.1    Honig, B.H.2
  • 20
    • 0027482287 scopus 로고
    • P22 Arc repressor: Enhanced expression of unstable mutants by addition of polar C-terminal sequences
    • Milla M.E., Brown B.M., Sauer R.T. P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences. Protein Sci. 2:1993;2198-2205
    • (1993) Protein Sci. , vol.2 , pp. 2198-2205
    • Milla, M.E.1    Brown, B.M.2    Sauer, R.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.