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Volumn 267, Issue 2, 1997, Pages 368-381

Electrostatic effects in homeodomain-DNA interactions

Author keywords

DNA binding proteins; Electrostatics; Homeodomain; Poisson Boltzmann; Protein DNA interactions

Indexed keywords

HOMEODOMAIN PROTEIN; MUTANT PROTEIN; SODIUM CHLORIDE;

EID: 0031588927     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0842     Document Type: Editorial
Times cited : (50)

References (67)
  • 1
    • 0028108227 scopus 로고
    • Differential DNA-binding specificity of the engrailed homeodomain: The role of residue 50
    • Ades S. E., Sauer R. T. Differential DNA-binding specificity of the engrailed homeodomain: the role of residue 50. Biochemistry. 33:1994;9187-9194.
    • (1994) Biochemistry , vol.33 , pp. 9187-9194
    • Ades, S.E.1    Sauer, R.T.2
  • 2
    • 0028810470 scopus 로고
    • Specificity of minor-groove and major-groove interactions in a homeodomain-DNA complex
    • Ades S. E., Sauer R. T. Specificity of minor-groove and major-groove interactions in a homeodomain-DNA complex. Biochemistry. 34:1995;14601-14608.
    • (1995) Biochemistry , vol.34 , pp. 14601-14608
    • Ades, S.E.1    Sauer, R.T.2
  • 3
    • 0001200075 scopus 로고
    • End effects in electrostatic potential of cylinders: Models for DNA fragments
    • Allison S. A. End effects in electrostatic potential of cylinders: models for DNA fragments. J. Phys. Chem. 98:1994;12091-12096.
    • (1994) J. Phys. Chem. , vol.98 , pp. 12091-12096
    • Allison, S.A.1
  • 4
    • 0028305457 scopus 로고
    • Prediction of pH-dependent properties of proteins
    • Antosiewicz J., McCammon J. A., Gilson M. K. Prediction of pH-dependent properties of proteins. J. Mol. Biol. 238:1994;415-436.
    • (1994) J. Mol. Biol. , vol.238 , pp. 415-436
    • Antosiewicz, J.1    McCammon, J.A.2    Gilson, M.K.3
  • 5
    • 0000339209 scopus 로고
    • Electrostatic effects in biological macromolecules
    • Bashford D. Electrostatic effects in biological macromolecules. Curr. Opin. Struct. Biol. 1:1991;175-184.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 175-184
    • Bashford, D.1
  • 7
    • 0027787519 scopus 로고
    • Determination of the nuclear magnetic resonance solution structure of an Antennapedia-DNA complex
    • Billeter M., Qian Y. Q., Otting G., Müller M., Gehring W. J., Wüthrich K. Determination of the nuclear magnetic resonance solution structure of an Antennapedia-DNA complex. J. Mol. Biol. 234:1993;1084-1097.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1084-1097
    • Billeter, M.1    Qian, Y.Q.2    Otting, G.3    Müller, M.4    Gehring, W.J.5    Wüthrich, K.6
  • 8
    • 0000071294 scopus 로고
    • A comprehensive classification of homeobox genes
    • D. Duboule. Oxford: Oxford University Press
    • Bürglin T. A comprehensive classification of homeobox genes. Duboule D. Guidebook to Homeobox Genes. 1993;27-72 Oxford University Press, Oxford.
    • (1993) Guidebook to Homeobox Genes , pp. 27-72
    • Bürglin, T.1
  • 9
    • 0027159255 scopus 로고
    • The X-ray structure of an atypical homeodomain present in the rat liver factor LFB1/HNF1 and implications for DNA binding
    • Ceska T. A., Lamers M., Monaci P., Nicosia A., Cortese R., Suck D. The X-ray structure of an atypical homeodomain present in the rat liver factor LFB1/HNF1 and implications for DNA binding. EMBO J. 12:1993;1805-1810.
    • (1993) EMBO J. , vol.12 , pp. 1805-1810
    • Ceska, T.A.1    Lamers, M.2    Monaci, P.3    Nicosia, A.4    Cortese, R.5    Suck, D.6
  • 11
    • 4243463817 scopus 로고
    • Electrostatics in biomolecular structure and dynamics
    • Davis M. E., McCammon J. A. Electrostatics in biomolecular structure and dynamics. Chem. Rev. 90:1990;509-521.
    • (1990) Chem. Rev. , vol.90 , pp. 509-521
    • Davis, M.E.1    McCammon, J.A.2
  • 12
    • 84986522972 scopus 로고
    • Dielectric boundary smoothing in finite difference solutions of the Poisson equation: An approach to improve accuracy and convergence
    • Davis M. E., McCammon J. A. Dielectric boundary smoothing in finite difference solutions of the Poisson equation: an approach to improve accuracy and convergence. J. Comp. Chem. 12:1991;909-912.
    • (1991) J. Comp. Chem. , vol.12 , pp. 909-912
    • Davis, M.E.1    McCammon, J.A.2
  • 13
    • 0026557592 scopus 로고
    • Antp-type homeodomains have distinct DNA binding specificities that correlate with their different regulatory functions in embryos
    • Dessain S., Gross T. C., Kuziora M. A., McGinnis W. Antp-type homeodomains have distinct DNA binding specificities that correlate with their different regulatory functions in embryos. EMBO J. 11:1992;991-1002.
    • (1992) EMBO J. , vol.11 , pp. 991-1002
    • Dessain, S.1    Gross, T.C.2    Kuziora, M.A.3    McGinnis, W.4
  • 14
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • Doig A. J., Sternberg M. E. Side-chain conformational entropy in protein folding. Protein Sci. 4:1995;2247-2251.
    • (1995) Protein Sci. , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, M.E.2
  • 16
    • 0029895487 scopus 로고    scopus 로고
    • The low dielectric interior of proteins is sufficient to cause major structural changes in DNA on association
    • Elcock A. H., McCammon J. A. The low dielectric interior of proteins is sufficient to cause major structural changes in DNA on association. J. Am. Chem. Soc. 118:1996;3787-3788.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3787-3788
    • Elcock, A.H.1    McCammon, J.A.2
  • 17
    • 0026660342 scopus 로고
    • Differential DNA sequence recognition is a determinant of specificity in homeotic gene action
    • Ekker S. C., von Kessler D. P., Beachy P. A. Differential DNA sequence recognition is a determinant of specificity in homeotic gene action. EMBO J. 11:1992;4059-4072.
    • (1992) EMBO J. , vol.11 , pp. 4059-4072
    • Ekker, S.C.1    Von Kessler, D.P.2    Beachy, P.A.3
  • 19
    • 33750208626 scopus 로고
    • The Poisson-Boltzmann equation and its application to polyelectrolytes
    • Fixman M. The Poisson-Boltzmann equation and its application to polyelectrolytes. J. Chem. Phys. 70:1979;4995-5005.
    • (1979) J. Chem. Phys. , vol.70 , pp. 4995-5005
    • Fixman, M.1
  • 20
    • 0026772477 scopus 로고
    • Polyelectrolytes in mixed salts: Scatchard plots obtained by means of Poisson-Boltzmann calculations
    • Fogolari F., Manzini G., Quadrifoglio F. Polyelectrolytes in mixed salts: Scatchard plots obtained by means of Poisson-Boltzmann calculations. Biophys. Chem. 43:1992;213-219.
    • (1992) Biophys. Chem. , vol.43 , pp. 213-219
    • Fogolari, F.1    Manzini, G.2    Quadrifoglio, F.3
  • 22
    • 0027746123 scopus 로고
    • Free energies calculated according to Manning's polyelectrolyte model compared with Poisson-Boltzmann predictions
    • Fogolari F., Cattarinussi S., Esposito G., Viglino P. Free energies calculated according to Manning's polyelectrolyte model compared with Poisson-Boltzmann predictions. J. Biomol. Struct. Dynam. 11:1993b;629-635.
    • (1993) J. Biomol. Struct. Dynam. , vol.11 , pp. 629-635
    • Fogolari, F.1    Cattarinussi, S.2    Esposito, G.3    Viglino, P.4
  • 24
    • 0021689084 scopus 로고
    • Polyelectrolyte effects on site-binding equilibria with application to the intercalation of drugs into DNA
    • Friedman R. A. G., Manning G. Polyelectrolyte effects on site-binding equilibria with application to the intercalation of drugs into DNA. Biopolymers. 23:1984;2671-2714.
    • (1984) Biopolymers , vol.23 , pp. 2671-2714
    • Friedman, R.A.G.1    Manning, G.2
  • 25
    • 0023239424 scopus 로고
    • Homeoboxes in the study of development
    • Gehring W. J. Homeoboxes in the study of development. Science. 236:1987;1245-1252.
    • (1987) Science , vol.236 , pp. 1245-1252
    • Gehring, W.J.1
  • 28
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution: Method and error assessment
    • Gilson M., Sharp K. A., Honig B. Calculating the electrostatic potential of molecules in solution: method and error assessment. J. Comp. Chem. 9:1987;327-335.
    • (1987) J. Comp. Chem. , vol.9 , pp. 327-335
    • Gilson, M.1    Sharp, K.A.2    Honig, B.3
  • 29
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha J.-H., Spolar R. S., Record M. T., Jr. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J. Mol. Biol. 209:1989;801-816.
    • (1989) J. Mol. Biol. , vol.209 , pp. 801-816
    • Ha, J.-H.1    Spolar, R.S.2    Record, M.T.3    Jr4
  • 30
    • 0029595248 scopus 로고
    • Structure of the even-skipped homeodomain complexed to AT-rich DNA: New perspectives on homeodomain specificity
    • Hirsch J. A., Aggarwal A. K. Structure of the even-skipped homeodomain complexed to AT-rich DNA: new perspectives on homeodomain specificity. EMBO J. 14:1995;6280-6291.
    • (1995) EMBO J. , vol.14 , pp. 6280-6291
    • Hirsch, J.A.1    Aggarwal, A.K.2
  • 31
    • 0024298689 scopus 로고
    • Divergent homeobox proteins recognize similar DNA sequences in Drosophila
    • Hoey T., Levine M. Divergent homeobox proteins recognize similar DNA sequences in Drosophila. Nature. 332:1988;858-861.
    • (1988) Nature , vol.332 , pp. 858-861
    • Hoey, T.1    Levine, M.2
  • 32
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., Nicholls A. Classical electrostatics in biology and chemistry. Science. 268:1995;1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 33
    • 0024580271 scopus 로고
    • The electrostatic potential of B-DNA
    • Jayaram B., Sharp K. A., Honig B. The electrostatic potential of B-DNA. Biopolymers. 28:1989;975-993.
    • (1989) Biopolymers , vol.28 , pp. 975-993
    • Jayaram, B.1    Sharp, K.A.2    Honig, B.3
  • 34
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen W. L., Tirado-Rives J. The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110:1988;1657-1666.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 35
  • 36
    • 0025188837 scopus 로고
    • Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: A framework for understanding homeodomain-DNA interactions
    • Kissinger C. R., Liu B., Martin-Blanco E., Kornberg T. B., Pabo C. O. Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: a framework for understanding homeodomain-DNA interactions. Cell. 63:1990;579-590.
    • (1990) Cell , vol.63 , pp. 579-590
    • Kissinger, C.R.1    Liu, B.2    Martin-Blanco, E.3    Kornberg, T.B.4    Pabo, C.O.5
  • 37
    • 0028200262 scopus 로고
    • Crystal structure of the oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
    • Klemm J. D., Rould M. A., Aurora R., Herr W., Pabo C. O. Crystal structure of the oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell. 77:1994;21-32.
    • (1994) Cell , vol.77 , pp. 21-32
    • Klemm, J.D.1    Rould, M.A.2    Aurora, R.3    Herr, W.4    Pabo, C.O.5
  • 38
    • 0028828745 scopus 로고
    • Crystal structure of the MATal/Matα2 homeodomain heterodimer bound to DNA
    • Li T., Stark M. R., Johnson A. D., Wolberger C. Crystal structure of the MATal/Matα2 homeodomain heterodimer bound to DNA. Science. 270:1995;262-269.
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 39
    • 0001200430 scopus 로고
    • Solving the finite-difference non-linear Poisson-Boltzmann equation
    • Luty B. A., Davis M. E., McCammon J. A. Solving the finite-difference non-linear Poisson-Boltzmann equation. J. Comp. Chem. 13:1992;114-118.
    • (1992) J. Comp. Chem. , vol.13 , pp. 114-118
    • Luty, B.A.1    Davis, M.E.2    McCammon, J.A.3
  • 40
    • 85050521214 scopus 로고
    • Biological applications of electrostatics calculations and Brownian dynamics simulations
    • Madura J. D., Davis M. E., Gilson M. K., Wade R., Luty B. A., McCammon J. A. Biological applications of electrostatics calculations and Brownian dynamics simulations. Rev. Comp. Chem. 5:1994;229-267.
    • (1994) Rev. Comp. Chem. , vol.5 , pp. 229-267
    • Madura, J.D.1    Davis, M.E.2    Gilson, M.K.3    Wade, R.4    Luty, B.A.5    McCammon, J.A.6
  • 42
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning G. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Quart. Rev. Biophys. 11:1978;179-246.
    • (1978) Quart. Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.1
  • 43
    • 0028246710 scopus 로고
    • Salt effects on ligand-DNA binding. Minor groove antibiotics
    • Misra V. K., Sharp K. A., Friedman R. A. G., Honig B. Salt effects on ligand-DNA binding. Minor groove antibiotics. J. Mol. Biol. 238:1994a;245-263.
    • (1994) J. Mol. Biol. , vol.238 , pp. 245-263
    • Misra, V.K.1    Sharp, K.A.2    Friedman, R.A.G.3    Honig, B.4
  • 44
    • 0028239626 scopus 로고
    • Salt effects on protein-DNA interactions. The λcI repressor and EcoRI endonuclease
    • Misra V. K., Hecht J. L., Sharp K. A., Friedman R. A. G., Honig B. Salt effects on protein-DNA interactions. The λcI repressor and EcoRI endonuclease. J. Mol. Biol. 238:1994b;264-280.
    • (1994) J. Mol. Biol. , vol.238 , pp. 264-280
    • Misra, V.K.1    Hecht, J.L.2    Sharp, K.A.3    Friedman, R.A.G.4    Honig, B.5
  • 45
    • 0010928616 scopus 로고
    • Continuum model calculations of solvation free energies: Accurate evaluation of electrostatic contributions
    • Mohan V., Davis M. E., McCammon J. A., Pettitt B. M. Continuum model calculations of solvation free energies: accurate evaluation of electrostatic contributions. J. Phys. Chem. 96:1992;6428-6431.
    • (1992) J. Phys. Chem. , vol.96 , pp. 6428-6431
    • Mohan, V.1    Davis, M.E.2    McCammon, J.A.3    Pettitt, B.M.4
  • 46
    • 33845378291 scopus 로고
    • Ionic distributions near polyelectrolytes. A comparison of theoretical approaches
    • Murthy C. S., Bacquet R. J., Rossky P. J. Ionic distributions near polyelectrolytes. A comparison of theoretical approaches. J. Phys. Chem. 89:1985;701-710.
    • (1985) J. Phys. Chem. , vol.89 , pp. 701-710
    • Murthy, C.S.1    Bacquet, R.J.2    Rossky, P.J.3
  • 47
    • 0028948325 scopus 로고
    • Structure-based design of transcription factors
    • Pomerantz J. L., Sharp P. A., Pabo C. O. Structure-based design of transcription factors. Science. 267:1995a;93-96.
    • (1995) Science , vol.267 , pp. 93-96
    • Pomerantz, J.L.1    Sharp, P.A.2    Pabo, C.O.3
  • 48
    • 0028862990 scopus 로고
    • Analysis of homeodomain fuction by structure-based design of a transcription factor
    • Pomerantz J. L., Pabo C. O., Sharp P. A. Analysis of homeodomain fuction by structure-based design of a transcription factor. Proc. Natl Acad. Sci. USA. 92:1995b;9752-9756.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9752-9756
    • Pomerantz, J.L.1    Pabo, C.O.2    Sharp, P.A.3
  • 49
    • 0025728614 scopus 로고
    • OPLS potential functions for nucleotide bases. Relative association constants of hydrogen-bonded base pairs in chloroform
    • Pranata J. S. G., Wierschke S. G., Jorgensen W. L. OPLS potential functions for nucleotide bases. Relative association constants of hydrogen-bonded base pairs in chloroform. J. Am. Chem. Soc. 113:1991;2810-2819.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 2810-2819
    • Pranata, J.S.G.1    Wierschke, S.G.2    Jorgensen, W.L.3
  • 50
    • 0017146579 scopus 로고
    • Ion effects on ligand-nucleic acid interactions
    • Record M. T., Jr, Lohman T. M., de Haseth P. Ion effects on ligand-nucleic acid interactions. J. Mol. Biol. 107:1976;145-158.
    • (1976) J. Mol. Biol. , vol.107 , pp. 145-158
    • Record, M.T.1    Jr2    Lohman, T.M.3    De Haseth, P.4
  • 51
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • Record M. T., Jr, Anderson C. F., Lohman T. M. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity. Quart. Rev. Biophys. 11:1978;103-178.
    • (1978) Quart. Rev. Biophys. , vol.11 , pp. 103-178
    • Record, M.T.1    Jr2    Anderson, C.F.3    Lohman, T.M.4
  • 52
    • 0026323912 scopus 로고
    • Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site specific complexes between proteins and helical DNA
    • Record M. T., Jr, Ha J.-H., Fisher M. A. Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site specific complexes between proteins and helical DNA. Methods Enzymol. 208:1991;291-343.
    • (1991) Methods Enzymol. , vol.208 , pp. 291-343
    • Record, M.T.1    Jr2    Ha, J.-H.3    Fisher, M.A.4
  • 54
    • 0028168562 scopus 로고
    • Design of a "minimal" homeodomain: The N-terminal arm modulates DNA binding affinity and stabilizes homeodomain structure
    • Shang Z., Ebu Isaac V., Li H., Patel L., Catron K. M., Curran T., Montelione G., Abate C. Design of a "minimal" homeodomain: the N-terminal arm modulates DNA binding affinity and stabilizes homeodomain structure. Proc. Nalt Acad. Sci. USA. 91:1994;8373-8377.
    • (1994) Proc. Nalt Acad. Sci. USA , vol.91 , pp. 8373-8377
    • Shang, Z.1    Ebu Isaac, V.2    Li, H.3    Patel, L.4    Catron, K.M.5    Curran, T.6    Montelione, G.7    Abate, C.8
  • 55
    • 0029068766 scopus 로고
    • Polyelectrolyte electrostatics: Salt dependence, entropic and enthalpic contribution to free energy in the nonlinear Poisson-Boltzmann model
    • Sharp K. A. Polyelectrolyte electrostatics: salt dependence, entropic and enthalpic contribution to free energy in the nonlinear Poisson-Boltzmann model. Biopolymers. 36:1995;227-243.
    • (1995) Biopolymers , vol.36 , pp. 227-243
    • Sharp, K.A.1
  • 56
    • 33751552991 scopus 로고
    • Calculating total electrostatic energies with the non-linear Poisson-Boltzmann equation
    • Sharp K. A., Honig B. Calculating total electrostatic energies with the non-linear Poisson-Boltzmann equation. J. Phys. Chem. 94:1990;7684-7692.
    • (1990) J. Phys. Chem. , vol.94 , pp. 7684-7692
    • Sharp, K.A.1    Honig, B.2
  • 57
    • 0029038105 scopus 로고
    • Salt effects on polyelectrolyte-ligand binding: Comparison of Poisson-Boltzmann and limiting law/counterion binding models
    • Sharp K. A., Friedman R. A., Misra V., Hecht J., Honig B. Salt effects on polyelectrolyte-ligand binding: comparison of Poisson-Boltzmann and limiting law/counterion binding models. Biopolymers. 36:1995;245-262.
    • (1995) Biopolymers , vol.36 , pp. 245-262
    • Sharp, K.A.1    Friedman, R.A.2    Misra, V.3    Hecht, J.4    Honig, B.5
  • 58
    • 0001300681 scopus 로고
    • Theory of Poisson Green's function for discontinuous dielectric media with an application to protein biophysics
    • Shaw P. B. Theory of Poisson Green's function for discontinuous dielectric media with an application to protein biophysics. Phys. Rev. Sect. A. 32:1985;2476-2487.
    • (1985) Phys. Rev. Sect. a , vol.32 , pp. 2476-2487
    • Shaw, P.B.1
  • 59
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R. S., Record M. T., Jr. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:1994;777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2    Jr3
  • 60
    • 0024397687 scopus 로고
    • A single amino acid can determine the DNA binding specificity of homeodomain proteins
    • Treisman J., Gönczy P., Vashishtha M., Harris E., Desplan C. A single amino acid can determine the DNA binding specificity of homeodomain proteins. Cell. 59:1989;553-562.
    • (1989) Cell , vol.59 , pp. 553-562
    • Treisman, J.1    Gönczy, P.2    Vashishtha, M.3    Harris, E.4    Desplan, C.5
  • 61
    • 0020475509 scopus 로고
    • Calculation of the electric potential in the active site cleft due to α-helix dipole
    • Warwicker J., Watson H. C. Calculation of the electric potential in the active site cleft due to α-helix dipole. J. Mol. Biol. 157:1982;671-679.
    • (1982) J. Mol. Biol. , vol.157 , pp. 671-679
    • Warwicker, J.1    Watson, H.C.2
  • 62
    • 84988053694 scopus 로고
    • An all atom forcefield for simulation of proteins and nucleic acids
    • Weiner S. J., Kollman P. A., Nguyen D. T., Case D. A. An all atom forcefield for simulation of proteins and nucleic acids. J. Comp. Chem. 77:1986;230-252.
    • (1986) J. Comp. Chem. , vol.77 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 63
    • 0029109864 scopus 로고
    • Cooperating to be different
    • Wilson D. S., Desplan C. Cooperating to be different. Curr. Biol. 5:1995;32-34.
    • (1995) Curr. Biol. , vol.5 , pp. 32-34
    • Wilson, D.S.1    Desplan, C.2
  • 64
    • 0029160486 scopus 로고
    • High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA
    • Wilson D. S., Guenther B., Desplan C., Kuriyan J. High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA. Cell. 82:1995;709-719.
    • (1995) Cell , vol.82 , pp. 709-719
    • Wilson, D.S.1    Guenther, B.2    Desplan, C.3    Kuriyan, J.4
  • 65
    • 0026002757 scopus 로고
    • Crystal structure of MAT α2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions
    • Wolberger C., Vershon A. K., Liu B., Johnson A. D., Pabo C. O. Crystal structure of MAT α2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell. 67:1991;517-528.
    • (1991) Cell , vol.67 , pp. 517-528
    • Wolberger, C.1    Vershon, A.K.2    Liu, B.3    Johnson, A.D.4    Pabo, C.O.5
  • 67
    • 0026619551 scopus 로고
    • Poisson-Boltzmann analysis of the λ repressor-operator interaction
    • Zacharias M., Luty B. A., Davis M. E., McCammon J. A. Poisson-Boltzmann analysis of the λ repressor-operator interaction. Biophys. J. 63:1992;1280-1285.
    • (1992) Biophys. J. , vol.63 , pp. 1280-1285
    • Zacharias, M.1    Luty, B.A.2    Davis, M.E.3    McCammon, J.A.4


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