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Volumn 96, Issue 4, 1999, Pages 587-597

Structure of a HoxB1-Pbx1 heterodimer bound to DNA: Role of the hexapeptide and a fourth homeodomain helix in complex formation

Author keywords

[No Author keywords available]

Indexed keywords

HOMEODOMAIN PROTEIN;

EID: 0033582545     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80662-5     Document Type: Article
Times cited : (288)

References (62)
  • 1
    • 0032473422 scopus 로고    scopus 로고
    • The novel homeoprotein Prep1 modulates Pbx-Hox protein cooperativity
    • Berthelsen, J., Zappavigna, V., Ferretti, E., Mavilio, F., and Blasi, F. (1998). The novel homeoprotein Prep1 modulates Pbx-Hox protein cooperativity. EMBO J. 17, 1434-1445.
    • (1998) EMBO J. , vol.17 , pp. 1434-1445
    • Berthelsen, J.1    Zappavigna, V.2    Ferretti, E.3    Mavilio, F.4    Blasi, F.5
  • 2
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 4
    • 1842339865 scopus 로고    scopus 로고
    • Analysis of TALE superclass homeobox genes (MEIS, PBC, KNOX, Iroquois, TGIF) reveals a novel domain conserved between plants and animals
    • Brüglin, T.R. (1997). Analysis of TALE superclass homeobox genes (MEIS, PBC, KNOX, Iroquois, TGIF) reveals a novel domain conserved between plants and animals. Nucleic Acids Res. 25, 4173-4180.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4173-4180
    • Brüglin, T.R.1
  • 5
    • 33744820336 scopus 로고
    • CCP4, Collaborative Computational Project Number 4
    • CCP4, Collaborative Computational Project Number 4. (1994). Acta Crystallogr. D50, 760.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760
  • 6
    • 0029890916 scopus 로고    scopus 로고
    • A structural model for a homeotic protein-extradenticle-DNA complex accounts for the choice of HOX protein in the heterodimer
    • Chan, S.K., and Mann, R.S. (1996). A structural model for a homeotic protein-extradenticle-DNA complex accounts for the choice of HOX protein in the heterodimer. Proc. Natl. Acad. Sci. USA 93, 5223-5228.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5223-5228
    • Chan, S.K.1    Mann, R.S.2
  • 7
    • 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., and Mann, R.S. (1994). The DNA binding specificity of ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein. Cell 78, 603-615.
    • (1994) Cell , vol.78 , pp. 603-615
    • Chan, S.-K.1    Jaffe, L.2    Capovilla, M.3    Botas, J.4    Mann, R.S.5
  • 8
    • 0028947525 scopus 로고
    • Pbx proteins display hexapeptidedependent cooperative DNA binding with a subset of Hox proteins
    • Chang, C.-P., Shen, W.-F., Rozenfeld, S., Lawrence, H.J., Largman, C., and Cleary, M.L (1995). Pbx proteins display hexapeptidedependent cooperative DNA binding with a subset of Hox proteins. Genes Dev. 9, 663-674.
    • (1995) Genes Dev. , vol.9 , pp. 663-674
    • Chang, C.-P.1    Shen, W.-F.2    Rozenfeld, S.3    Lawrence, H.J.4    Largman, C.5    Cleary, M.L.6
  • 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., and Cleary, M.L. (1996). Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus. Mol. Cell. Biol. 16, 1734-1745.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1734-1745
    • Chang, C.P.1    Brocchieri, L.2    Shen, W.F.3    Largman, C.4    Cleary, M.L.5
  • 10
    • 0031031879 scopus 로고    scopus 로고
    • The Hoxcooperativity motif of the chimeric oncoprotein E2a-Pbx1 is necessary and sufficient for oncogenesis
    • Chang, C.P., de Vivo, I., and Cleary, M.L. (1997a). The Hoxcooperativity motif of the chimeric oncoprotein E2a-Pbx1 is necessary and sufficient for oncogenesis. Mol. Cell. Biol. 17, 81-88.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 81-88
    • Chang, C.P.1    De Vivo, I.2    Cleary, M.L.3
  • 11
    • 0030813558 scopus 로고    scopus 로고
    • Meis proteins are major in vivo DNA binding partners for wild-type but not chimeric Pbx proteins
    • Chang, C.P., Jacobs, Y., Nakamura, T., Jenkins, N.A., Copeland, N.G., and Cleary, M.L. (1997b). Meis proteins are major in vivo DNA binding partners for wild-type but not chimeric Pbx proteins. Mol. Cell Biol. 17, 5679-5687.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 5679-5687
    • Chang, C.P.1    Jacobs, Y.2    Nakamura, T.3    Jenkins, N.A.4    Copeland, N.G.5    Cleary, M.L.6
  • 14
    • 0030923678 scopus 로고    scopus 로고
    • Functional dissection of a transcriptionally active, target-specific Hox-Pbx complex
    • Di Rocco, G., Mavilio, F., and Zappavigna, V. (1997). Functional dissection of a transcriptionally active, target-specific Hox-Pbx complex. EMBO J. 16, 3644-3654.
    • (1997) EMBO J. , vol.16 , pp. 3644-3654
    • Di Rocco, G.1    Mavilio, F.2    Zappavigna, V.3
  • 15
    • 0004107629 scopus 로고
    • Duboule, D., ed. Oxford: Oxford University Press
    • Duboule, D., ed. (1994). Guidebook to the Homeobox Genes. (Oxford: Oxford University Press).
    • (1994) Guidebook to the Homeobox Genes
  • 17
    • 0031851485 scopus 로고    scopus 로고
    • Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex
    • Fraenkel, E., and Pabo, C.O. (1998). Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex. Nat. Struct. Biol. 5, 692-697.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 692-697
    • Fraenkel, E.1    Pabo, C.O.2
  • 18
    • 0032573434 scopus 로고    scopus 로고
    • Engrailed homeodomain-DNA complex at 2.2 Å: A detailed view of the interface and comparison with other engrailed structures
    • Fraenkel, E., Rould, R., Chambers, K., and Pabo, C.O. (1998). Engrailed homeodomain-DNA complex at 2.2 Å: a detailed view of the interface and comparison with other engrailed structures. J. Mol. Biol. 27, 351-361.
    • (1998) J. Mol. Biol. , vol.27 , pp. 351-361
    • Fraenkel, E.1    Rould, R.2    Chambers, K.3    Pabo, C.O.4
  • 20
    • 0032557549 scopus 로고    scopus 로고
    • A conserved C-terminal domain in PBX increases DNA binding by the PBX homeodomain and is not a primary site of contact for the YPWM motif of HOXA1
    • Green, N.C., Rambaldi, I., Teakles, J., and Featherstone, M.S. (1998). A conserved C-terminal domain in PBX increases DNA binding by the PBX homeodomain and is not a primary site of contact for the YPWM motif of HOXA1. J. Biol. Chem. 273, 13273-13279.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13273-13279
    • Green, N.C.1    Rambaldi, I.2    Teakles, J.3    Featherstone, M.S.4
  • 21
    • 0031449215 scopus 로고    scopus 로고
    • Synergistic activation of a Drosophila enhancer by HOM/EXD and DPP signaling
    • Grieder, N.C., Marty, T., Ryoo, H.D., Mann, R.S., and Affolter, M. (1997). Synergistic activation of a Drosophila enhancer by HOM/EXD and DPP signaling. EMBO J. 16, 7402-7410.
    • (1997) EMBO J. , vol.16 , pp. 7402-7410
    • Grieder, N.C.1    Marty, T.2    Ryoo, H.D.3    Mann, R.S.4    Affolter, M.5
  • 22
    • 0029595248 scopus 로고
    • Structure of even skipped homeodomain complexed to at rich DNA: New perspectives on homeodomain specificity
    • Hirsch, J.A., and Aggarwal, A.K. (1995). Structure of even skipped homeodomain complexed to AT rich DNA: new perspectives on homeodomain specificity. EMBO J. 14, 6280-6291.
    • (1995) EMBO J. , vol.14 , pp. 6280-6291
    • Hirsch, J.A.1    Aggarwal, A.K.2
  • 23
    • 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., and Krasnow, M.A. (1995). 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) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 739-743
    • Johnson, F.B.1    Parker, E.2    Krasnow, M.A.3
  • 24
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 25
    • 0025137176 scopus 로고
    • A new homeobox gene contributes the DNA binding domain of the t(1:19) translocation protein in pre-B ALL
    • Kamps, M.P., Murre, C., Sun, X., and Baltimore, D. (1990). A new homeobox gene contributes the DNA binding domain of the t(1:19) translocation protein in pre-B ALL. Cell 60, 547-555.
    • (1990) Cell , vol.60 , pp. 547-555
    • Kamps, M.P.1    Murre, C.2    Sun, X.3    Baltimore, D.4
  • 26
    • 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., and Pabo, C.O. (1990). Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: a framework for understanding homeodomain-DNA interactions. Cell 63, 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
  • 27
    • 0030025170 scopus 로고    scopus 로고
    • Oct-1 POU domain-DNA interactions: Cooperative binding of isolated subdomains and effects of covalent linkage
    • Klemm, J.D., and Pabo, C.O. (1996). Oct-1 POU domain-DNA interactions: cooperative binding of isolated subdomains and effects of covalent linkage. Genes Dev. 10, 27-36.
    • (1996) Genes Dev. , vol.10 , pp. 27-36
    • Klemm, J.D.1    Pabo, C.O.2
  • 28
    • 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., and Pabo, C.O. (1994). Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell 77, 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
  • 29
    • 0029118224 scopus 로고
    • The pentapeptide motif of Hox proteins is required for cooperative DNA binding with Pbx1, physically contacts Pbx1, and enhances DNA binding by Pbx1
    • Knoepfler, P.S., and Kamps, M.P. (1995). The pentapeptide motif of Hox proteins is required for cooperative DNA binding with Pbx1, physically contacts Pbx1, and enhances DNA binding by Pbx1. Mol. Cell. Biol. 75, 5811-5819.
    • (1995) Mol. Cell. Biol. , vol.75 , pp. 5811-5819
    • Knoepfler, P.S.1    Kamps, M.P.2
  • 30
    • 0031446339 scopus 로고    scopus 로고
    • Meisl and pKnox1 bind DNA cooperatively with Pbx1 utilizing an interaction surface disrupted in oncoprotein E2a-Pbx1
    • Knoepfler, P.S., Calvo, K.R., Chen, H., Antonarakis, S.E., and Kamps, M.P. (1997). Meisl and pKnox1 bind DNA cooperatively with Pbx1 utilizing an interaction surface disrupted in oncoprotein E2a-Pbx1. Proc. Natl. Acad. Sci. USA 94, 14553-14558.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14553-14558
    • Knoepfler, P.S.1    Calvo, K.R.2    Chen, H.3    Antonarakis, S.E.4    Kamps, M.P.5
  • 31
    • 0026321622 scopus 로고
    • DNA binding specificity of homeodomains
    • Laughon, A. (1991). DNA binding specificity of homeodomains. Biochemistry 30, 11357-11367.
    • (1991) Biochemistry , vol.30 , pp. 11357-11367
    • Laughon, A.1
  • 32
    • 0024058085 scopus 로고
    • The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids
    • Lavery, R., and Sklenar, H. (1988). The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids. J. Biomol. Struct. Dyn. 6, 63-91.
    • (1988) J. Biomol. Struct. Dyn. , vol.6 , pp. 63-91
    • Lavery, R.1    Sklenar, H.2
  • 33
    • 0028303736 scopus 로고
    • Fusion with E2A alters the transcriptional properties of the homeodomain protein PBX1 in t(1;19) leukemias
    • LeBrun, D.P., and Cleary, M.L. (1994). Fusion with E2A alters the transcriptional properties of the homeodomain protein PBX1 in t(1;19) leukemias. Oncogene 9, 1641-1647.
    • (1994) Oncogene , vol.9 , pp. 1641-1647
    • LeBrun, D.P.1    Cleary, M.L.2
  • 34
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MATα2 homeodomain heterodimer bound to DNA
    • Li, T., Stark, M.R., Johnson, A.D., and Wolberger, C. (1995). Crystal structure of the MATa1/MATα2 homeodomain heterodimer bound to DNA. Science 270, 262-269.
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 35
    • 0029966661 scopus 로고    scopus 로고
    • Structural determinants within Pbx1 that mediate cooperative DNA binding with pentapeptide-containing Hox proteins: Proposal for a model of a Pbx1-Hox-DNA complex
    • Lu, Q., and Kamps, M.P. (1996). Structural determinants within Pbx1 that mediate cooperative DNA binding with pentapeptide-containing Hox proteins: proposal for a model of a Pbx1-Hox-DNA complex. Mol. Cell. Biol. 16, 1632-1640.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1632-1640
    • Lu, Q.1    Kamps, M.P.2
  • 36
    • 0031019639 scopus 로고    scopus 로고
    • Heterodimerization of Hox proteins with Pbx1 and oncoprotein E2a-Pbx1 generates unique DNA-binding specifies at nucleotides predicted to contact the N-terminal arm of the Hox homeodomain - Demonstration of Hox-dependent targeting of E2a-Pbx1 in vivo
    • Lu, Q., and Kamps, M.P. (1997). Heterodimerization of Hox proteins with Pbx1 and oncoprotein E2a-Pbx1 generates unique DNA-binding specifies at nucleotides predicted to contact the N-terminal arm of the Hox homeodomain - demonstration of Hox-dependent targeting of E2a-Pbx1 in vivo. Oncogene 14, 75-83.
    • (1997) Oncogene , vol.14 , pp. 75-83
    • Lu, Q.1    Kamps, M.P.2
  • 37
    • 0028231938 scopus 로고
    • Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation
    • Lu, Q., Wright, D.D., and Kamps, M.P. (1994). Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation. Mol. Cell. Biol. 14, 3938-3948.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3938-3948
    • Lu, Q.1    Wright, D.D.2    Kamps, M.P.3
  • 38
    • 0029054140 scopus 로고
    • Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively with the products of multiple murine Hox genes, some of which are themselves oncogenes
    • Lu, Q., Knoepfler, P.S., Scheele, J., Wright, D.D., and Kamps, M.P. (1995). Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively with the products of multiple murine Hox genes, some of which are themselves oncogenes. Mol. Cell Biol. 15, 3786-3795.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 3786-3795
    • Lu, Q.1    Knoepfler, P.S.2    Scheele, J.3    Wright, D.D.4    Kamps, M.P.5
  • 39
    • 0030746837 scopus 로고    scopus 로고
    • Cross-regulation in the mouse HoxB complex: The expression of Hoxb2 in rhombomere 4 is regulated by Hoxb1
    • Maconochie, M.K., Nonchev, S., Studer, M., Chan, S.-K., Pöpperl, H., Sham, M.H., Mann, R.S., and Krumlauf, R. (1997). Cross-regulation in the mouse HoxB complex: the expression of Hoxb2 in rhombomere 4 is regulated by Hoxb1. Genes Dev. 11, 1883-1895.
    • (1997) Genes Dev. , vol.11 , pp. 1883-1895
    • Maconochie, M.K.1    Nonchev, S.2    Studer, M.3    Chan, S.-K.4    Pöpperl, H.5    Sham, M.H.6    Mann, R.S.7    Krumlauf, R.8
  • 40
    • 0029898760 scopus 로고    scopus 로고
    • Extra specificity from extradenticle: The partnership between Hox and exd/pbx homeodomain proteins
    • Mann, R.S., and Chan, S.-K. (1996). Extra specificity from extradenticle: the partnership between Hox and exd/pbx homeodomain proteins. Trends Genet. 12, 258-262.
    • (1996) Trends Genet. , vol.12 , pp. 258-262
    • Mann, R.S.1    Chan, S.-K.2
  • 41
    • 0026504525 scopus 로고
    • Homeobox genes and axial patterning
    • McGinnis, W., and Krumlauf, R. (1992). Homeobox genes and axial patterning. Cell 68, 283-302.
    • (1992) Cell , vol.68 , pp. 283-302
    • McGinnis, W.1    Krumlauf, R.2
  • 43
    • 0030753645 scopus 로고    scopus 로고
    • Pbx raises the DNA binding specificity but not the selectivity of antennapedia Hox proteins
    • Neuteboom, S.T., and Murre, C. (1997). Pbx raises the DNA binding specificity but not the selectivity of antennapedia Hox proteins. Mol. Cell Biol. 17, 4696-4706.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 4696-4706
    • Neuteboom, S.T.1    Murre, C.2
  • 44
    • 0029079663 scopus 로고
    • The hexapeptide LFPWM R in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins
    • Neuteboom, S.T., Peltenburg, L.T., van Dijk, M.A., and Murre, C. (1995). The hexapeptide LFPWM R in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins. Proc. Natl. Acad. Sci. USA 92, 9166-9170.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9166-9170
    • Neuteboom, S.T.1    Peltenburg, L.T.2    Van Dijk, M.A.3    Murre, C.4
  • 45
    • 0025064238 scopus 로고
    • Chromosomal translocation t(1;19) results in synthesis of a homeodomain fusion mRNA that codes for a potential chimeric transcription factor
    • Nourse, J., Mellentin, J.D., Galili, N., Wilkinson, J., Stanbridge, E., Smith, S.D., and Cleary, M.L. (1990). Chromosomal translocation t(1;19) results in synthesis of a homeodomain fusion mRNA that codes for a potential chimeric transcription factor. Cell 60, 535-545.
    • (1990) Cell , vol.60 , pp. 535-545
    • Nourse, J.1    Mellentin, J.D.2    Galili, N.3    Wilkinson, J.4    Stanbridge, E.5    Smith, S.D.6    Cleary, M.L.7
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otinowski, Z., and Minor, W. (1997). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otinowski, Z.1    Minor, W.2
  • 47
    • 0025365228 scopus 로고
    • Mutations in the Drosophila gene extradenticle affect the way specific homeodomain proteins regulate segmental identity
    • Peifer, M., and Wieschaus, E. (1990). Mutations in the Drosophila gene extradenticle affect the way specific homeodomain proteins regulate segmental identity. Genes Dev. 4, 1209-1223.
    • (1990) Genes Dev. , vol.4 , pp. 1209-1223
    • Peifer, M.1    Wieschaus, E.2
  • 48
    • 0030894303 scopus 로고    scopus 로고
    • Specific residues in the Pbx homeodomain differentially modulate the DNA-binding activity of ox and Engrailed proteins
    • Peltenburg, LT., and Murre, C. (1997). Specific residues in the Pbx homeodomain differentially modulate the DNA-binding activity of ox and Engrailed proteins. Development 124, 1089-1098.
    • (1997) Development , vol.124 , pp. 1089-1098
    • Peltenburg, L.T.1    Murre, C.2
  • 49
    • 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., and Featherstone, M.S. (1997). 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) J. Biol. Chem. , vol.272 , pp. 8635-8643
    • Phelan, M.L.1    Featherstone, M.S.2
  • 50
    • 0025754413 scopus 로고
    • Secondary structure of the homeodomain of yeast alpha 2 represser determined by NMR spectroscopy
    • Phillips, C.L., Vershon, A.K., Johnson, A.D., and Dahlquist, F.W. (1991). Secondary structure of the homeodomain of yeast alpha 2 represser determined by NMR spectroscopy. Genes Dev. 5, 764-772.
    • (1991) Genes Dev. , vol.5 , pp. 764-772
    • Phillips, C.L.1    Vershon, A.K.2    Johnson, A.D.3    Dahlquist, F.W.4
  • 51
    • 0029055810 scopus 로고
    • Segmental expression of Hoxb-1 is controlled by a highly conserved autoregulatory loop dependent upon exd/pbx
    • Popperl, H., Bienz, M., Studer, M., Chan, S.K., Aparicio, S., Brenner, S., Mann, R.S., and Krumlauf, R. (1995). Segmental expression of Hoxb-1 is controlled by a highly conserved autoregulatory loop dependent upon exd/pbx. Cell 81, 1031-1042.
    • (1995) Cell , vol.81 , pp. 1031-1042
    • Popperl, H.1    Bienz, M.2    Studer, M.3    Chan, S.K.4    Aparicio, S.5    Brenner, S.6    Mann, R.S.7    Krumlauf, R.8
  • 52
    • 0026482958 scopus 로고
    • NMR structure determination reveals that the homeodomain is connected through a flexible linker to the main body in the Drosophila Antennapedia protein
    • Qian, Y.Q., Otting, G., Furukubo-Tokunaga, K., Affolter, M., Gehring, W.J., and Wüthrich, K. (1992). NMR structure determination reveals that the homeodomain is connected through a flexible linker to the main body in the Drosophila Antennapedia protein. Proc. Natl. Acad. Sci. USA 89, 10738-10742.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10738-10742
    • Qian, Y.Q.1    Otting, G.2    Furukubo-Tokunaga, K.3    Affolter, M.4    Gehring, W.J.5    Wüthrich, K.6
  • 54
    • 0027519720 scopus 로고
    • Extradenticle, a regulator of homeotic gene activity, is a homolog of the homeobox-containing human proto-oncogene pbx1
    • Rauskolb, C., Peifer, M., and Wieschaus, E. (1993). Extradenticle, a regulator of homeotic gene activity, is a homolog of the homeobox-containing human proto-oncogene pbx1. Cell 74, 1101-1112.
    • (1993) Cell , vol.74 , pp. 1101-1112
    • Rauskolb, C.1    Peifer, M.2    Wieschaus, E.3
  • 55
    • 0030725941 scopus 로고    scopus 로고
    • Nuclear translocation of extradenticle requires homothorax, which encodes an extradenticle-related homeodomain protein
    • Rieckhof, G.E., Casares, F., Ryoo, H.D., Abu-Shaar, M., and Mann, R.S. (1997). Nuclear translocation of extradenticle requires homothorax, which encodes an extradenticle-related homeodomain protein. Cell 91, 171-183.
    • (1997) Cell , vol.91 , pp. 171-183
    • Rieckhof, G.E.1    Casares, F.2    Ryoo, H.D.3    Abu-Shaar, M.4    Mann, R.S.5
  • 57
    • 0028658407 scopus 로고
    • Elongation of helix III of the NK-2 homeodomain upon binding to DNA: A secondary structure study by NMR
    • Tsao, D.H., Gruschus, J.M., Wang, L.H., Nirenberg, M., and Ferretti, U.A. (1994). Elongation of helix III of the NK-2 homeodomain upon binding to DNA: a secondary structure study by NMR. Biochemistry 33, 15053-15060.
    • (1994) Biochemistry , vol.33 , pp. 15053-15060
    • Tsao, D.H.1    Gruschus, J.M.2    Wang, L.H.3    Nirenberg, M.4    Ferretti, U.A.5
  • 58
    • 0030609996 scopus 로고    scopus 로고
    • Engrailed ([Gln50-]Lys) homeodomain-DNA complex at 1.9 Å resolution - Structural basis for enhanced affinity and altered specificity
    • Tucker-Kellogg, L., Rould, M.A., Chambers, K.A., Ades, S.E., Sauer, R.T., and Pabo, C.O. (1997). Engrailed ([Gln50-]Lys) homeodomain-DNA complex at 1.9 Å resolution - structural basis for enhanced affinity and altered specificity. Structure 5, 1047-1054.
    • (1997) Structure , vol.5 , pp. 1047-1054
    • Tucker-Kellogg, L.1    Rould, M.A.2    Chambers, K.A.3    Ades, S.E.4    Sauer, R.T.5    Pabo, C.O.6
  • 59
    • 0028169993 scopus 로고
    • Extradenticle raises the DNA binding specificity of homeodomain selector gene products
    • van Dijk, M.A., and Murre, C. (1994). extradenticle raises the DNA binding specificity of homeodomain selector gene products. Cell 78, 617-624.
    • (1994) Cell , vol.78 , pp. 617-624
    • Van Dijk, M.A.1    Murre, C.2
  • 60
    • 0027176915 scopus 로고
    • Pbx1 is converted into a transcriptional activator upon acquiring the N-terminal region of E2A in pre-B-cell acute lymphoblastic leukemia
    • van Dijk, M.A., Voorhoeve, P.M., and Murre, C. (1993). Pbx1 is converted into a transcriptional activator upon acquiring the N-terminal region of E2A in pre-B-cell acute lymphoblastic leukemia. Proc. Natl. Acad. Sci. USA 90, 6061-6065.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6061-6065
    • Van Dijk, M.A.1    Voorhoeve, P.M.2    Murre, C.3
  • 61
    • 0029160486 scopus 로고
    • High resolution crystal structure of a paired (PAX) class cooperative homeodomain dimer on DNA
    • Wilson, D.S., Guenther, B., Desplan, C., and Kuriyan, J. (1995). High resolution crystal structure of a paired (PAX) class cooperative homeodomain dimer on DNA. Cell 82, 709-719.
    • (1995) Cell , vol.82 , pp. 709-719
    • Wilson, D.S.1    Guenther, B.2    Desplan, C.3    Kuriyan, J.4
  • 62
    • 0026002757 scopus 로고
    • Crystal structure of a MATα2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions
    • Wolberger, C., Vershon, A.K., Liu, B., Johnson, A.D., and Pabo, C.O. (1991). Crystal structure of a MATα2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell 67, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.