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Volumn 397, Issue 6721, 1999, Pages 714-719

Structure of a DNA-bound Ultrabithorax-Extradenticle homeodomain complex

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HOMEODOMAIN PROTEIN;

EID: 0033602242     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/17833     Document Type: Article
Times cited : (276)

References (30)
  • 1
    • 0018240421 scopus 로고
    • A gene complex controlling segmentation in Drosophila
    • Lewis, E. B. A gene complex controlling segmentation in Drosophila. Nature 276, 565-570 (1978).
    • (1978) Nature , vol.276 , pp. 565-570
    • Lewis, E.B.1
  • 2
    • 0026504525 scopus 로고
    • Homeobox genes and axial patterning
    • McGinnis, W. & Krumlauf, R. Homeobox genes and axial patterning. Cell 68, 283-302 (1992).
    • (1992) Cell , vol.68 , pp. 283-302
    • McGinnis, W.1    Krumlauf, R.2
  • 3
    • 0029898760 scopus 로고    scopus 로고
    • Extra specificity from extradenticle: The partnership between HOX and exd/pbx homeodomain proteins
    • Mann, R. S. & Chan, S.-K. Extra specificity from extradenticle: the partnership between HOX and exd/pbx homeodomain proteins. Trends Genet. 12, 258-262 (1996).
    • (1996) Trends Genet. , vol.12 , pp. 258-262
    • Mann, R.S.1    Chan, S.-K.2
  • 4
    • 0029379593 scopus 로고
    • The specificity of homeotic gene function
    • Mann, R. S. The specificity of homeotic gene function. Bioessays 17, 855-863 (1995).
    • (1995) Bioessays , vol.17 , pp. 855-863
    • Mann, R.S.1
  • 7
    • 0029966661 scopus 로고    scopus 로고
    • Structural determinants of Pbx1 mediating cooperative DNA-binding with pentapeptide-containing HOX proteins
    • Lu, Q. & Kamps, M. Structural determinants of Pbx1 mediating cooperative DNA-binding with pentapeptide-containing HOX proteins. Mol. Cell. Biol. 16, 1632-1640 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1632-1640
    • Lu, Q.1    Kamps, M.2
  • 8
    • 0029890916 scopus 로고    scopus 로고
    • A structural model for an extradenticle-HOX-DNA complex accounts for the choice of HOX protein in the heterodimer
    • Chan, S.-K. & Mann, R. S. A structural model for an extradenticle-HOX-DNA complex accounts for the choice of HOX protein in the heterodimer. Proc. Natl Acad. Sci. USA 93, 5223-5228 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5223-5228
    • Chan, S.-K.1    Mann, R.S.2
  • 9
    • 0029939199 scopus 로고    scopus 로고
    • Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus
    • Chang, C. P., Brocchieri, L., Shen, W. F., Largman, C. & Clearly, M. L. Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus. Mol. Cell. Biol. 16, 1734-1745 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1734-1745
    • Chang, C.P.1    Brocchieri, L.2    Shen, W.F.3    Largman, C.4    Clearly, M.L.5
  • 10
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA
    • Li, T., Stark, M. R., Johnson, A. D. & Wolberger, C. Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA. Science 270, 262-269 (1995).
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 11
    • 0027966927 scopus 로고
    • The DNA binding specificity of Ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein
    • Chan, S. K., Jaffe, L., Capovilla, M., Botas, J. & Mann, R. S. The DNA binding specificity of Ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein. Cell 78, 603-615 (1994).
    • (1994) Cell , vol.78 , pp. 603-615
    • Chan, S.K.1    Jaffe, L.2    Capovilla, M.3    Botas, J.4    Mann, R.S.5
  • 12
    • 0031851485 scopus 로고    scopus 로고
    • Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex
    • Fraenkel, E. & Pabo, C. O. Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex. Nature Struct. Biol. 5, 692-697 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 692-697
    • Fraenkel, E.1    Pabo, C.O.2
  • 13
    • 0025785350 scopus 로고
    • Murine genes related to teh Drosophila AbdB homeotic gene are sequentially expressed during development of the posterior part of the body
    • Izpisua-Belmonte, J. C., Falkenstein, H., Dolle, P., Renucci, A. & Duboule, D. Murine genes related to teh Drosophila AbdB homeotic gene are sequentially expressed during development of the posterior part of the body. EMBO J. 10, 2279-2289 (1991).
    • (1991) EMBO J. , vol.10 , pp. 2279-2289
    • Izpisua-Belmonte, J.C.1    Falkenstein, H.2    Dolle, P.3    Renucci, A.4    Duboule, D.5
  • 14
    • 0028809109 scopus 로고
    • Extradenticle protein is a selective cofactor for the Drosophila homeotics: Role of the homeodomain and YPWM amino acid motif in the interaction
    • Johnson, F. B., Parker, E. & Krasnow, M. A. Extradenticle protein is a selective cofactor for the Drosophila homeotics: role of the homeodomain and YPWM amino acid motif in the interaction. Proc. Natl Acad. Sci. USA 92, 739-743 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 739-743
    • Johnson, F.B.1    Parker, E.2    Krasnow, M.A.3
  • 15
    • 0029925624 scopus 로고    scopus 로고
    • An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif
    • Chan, S.-K., Pöpperl, H., Krumlauf, R. & Mann, R. S. An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif. EMBO J. 15, 2477-2488 (1996).
    • (1996) EMBO J. , vol.15 , pp. 2477-2488
    • Chan, S.-K.1    Pöpperl, H.2    Krumlauf, R.3    Mann, R.S.4
  • 16
    • 0028858251 scopus 로고
    • Extradenticle determines segmental identities throughout development
    • Rauskolb, C., Smith, K., Peifer, M. & Wieschaus, E. Extradenticle determines segmental identities throughout development. Development 121, 3663-3671 (1995).
    • (1995) Development , vol.121 , pp. 3663-3671
    • Rauskolb, C.1    Smith, K.2    Peifer, M.3    Wieschaus, E.4
  • 17
    • 0030025170 scopus 로고    scopus 로고
    • Oct-1 POU domain-DNA interactions: Cooperative binding of isolated subdomains and effects of covalent linkage
    • Klemm, J. D. & Pabo, C. O. Oct-1 POU domain-DNA interactions: cooperative binding of isolated subdomains and effects of covalent linkage. Genes Dev. 10, 27-36 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 27-36
    • Klemm, J.D.1    Pabo, C.O.2
  • 18
    • 0030887351 scopus 로고    scopus 로고
    • Distinct HOX N-terminal arm residues are responsible for specificity of DNA recognition by HOX monomers and HOX-PBX heterodimers
    • Phelan, M. L. & Featherstone, M. S. Distinct HOX N-terminal arm residues are responsible for specificity of DNA recognition by HOX monomers and HOX-PBX heterodimers. J. Biol. Chem. 272, 8635-8643 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 8635-8643
    • Phelan, M.L.1    Featherstone, M.S.2
  • 19
    • 0024284650 scopus 로고
    • Recognition of a DNa operator by the repressor of phage 434: A view at high resolution
    • Aggarwal, A. K., Rodgers, D. W., Drottar, M., Ptashne, M. & Harrison, S. C. Recognition of a DNA operator by the repressor of phage 434: a view at high resolution. Science 242, 899-907 (1988).
    • (1988) Science , vol.242 , pp. 899-907
    • Aggarwal, A.K.1    Rodgers, D.W.2    Drottar, M.3    Ptashne, M.4    Harrison, S.C.5
  • 20
    • 0024294634 scopus 로고
    • Crystal structure of trp repressor/operator complex at atomic resolution
    • Otwinowski, Z. et al. Crystal structure of trp repressor/operator complex at atomic resolution. Nature 335, 321-329 (1988).
    • (1988) Nature , vol.335 , pp. 321-329
    • Otwinowski, Z.1
  • 21
    • 0032509980 scopus 로고    scopus 로고
    • Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex
    • Tan, S. & Richmond, T. J. Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex. Nature 391, 660-666 (1998).
    • (1998) Nature , vol.391 , pp. 660-666
    • Tan, S.1    Richmond, T.J.2
  • 22
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S. & Chotia, C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204, 155-164 (1988).
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chotia, C.3
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 25
    • 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, 6280-6291 (1995).
    • (1995) EMBO J. , vol.14 , pp. 6280-6291
    • Hirsch, J.A.1    Aggarwal, A.K.2
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy atom parameter refinement for the mutliple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy atom parameter refinement for the mutliple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 29
    • 0027609916 scopus 로고
    • Setor: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S. V. Setor: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138 (1993).
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 30
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.