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Volumn 7, Issue 4, 1996, Pages 392-396

Protein interactions of homeodomain proteins

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; HOMEODOMAIN PROTEIN;

EID: 0030220608     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(96)80113-3     Document Type: Article
Times cited : (13)

References (36)
  • 2
    • 0000970094 scopus 로고
    • The evolution of homeobox genes
    • Edited by Arai R, Kato M, Doi Y. Tokyo: The National Science Museum Foundation
    • Bürglin TR: The evolution of homeobox genes. In Biodiversity and Evolution. Edited by Arai R, Kato M, Doi Y. Tokyo: The National Science Museum Foundation; 1995:291-336.
    • (1995) In Biodiversity and Evolution , pp. 291-336
    • Bürglin, T.R.1
  • 3
    • 0024407460 scopus 로고
    • The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: Comparison with prokaryotic repressors
    • Qian YQ, Billeter M, Otting G, Müller M, Gehring WJ, Wüthrich K. The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors. Cell. 59:1989;573-580.
    • (1989) Cell , vol.59 , pp. 573-580
    • Qian, Y.Q.1    Billeter, M.2    Otting, G.3    Müller, M.4    Gehring, W.J.5    Wüthrich, K.6
  • 4
    • 0025188837 scopus 로고
    • Crystal structure of an engrailed homeodomain - DNA complex at 2.8 Å resolution: A framework for understanding homeodomain - DNA interactions
    • Kissinger CR, Liu BS, Martin-Blanco E, Kornberg TB, Pabo CO. 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.S.2    Martin-Blanco, E.3    Kornberg, T.B.4    Pabo, C.O.5
  • 5
    • 0025754413 scopus 로고
    • Secondary structure of the homeodomain of yeast α2 repressor determined by NMR spectroscopy
    • Phillips CL, Vershon AK, Johnson AD, Dahlquist FW. Secondary structure of the homeodomain of yeast α2 repressor determined by NMR spectroscopy. Genes Dev. 5:1991;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
  • 6
    • 0024997404 scopus 로고
    • Protein - DNA contacts in the structure of a homeodomain - DNA complex determined by nuclear magnetic resonance spectroscopy in solution
    • Otting G, Qian YQ, Billeter M, Müller M, Affolter M, Gehring WJ, Wüthrich K. Protein - DNA contacts in the structure of a homeodomain - DNA complex determined by nuclear magnetic resonance spectroscopy in solution. EMBO J. 9:1990;3085-3092.
    • (1990) EMBO J , vol.9 , pp. 3085-3092
    • Otting, G.1    Qian, Y.Q.2    Billeter, M.3    Müller, M.4    Affolter, M.5    Gehring, W.J.6    Wüthrich, K.7
  • 7
    • 0026002757 scopus 로고
    • Crystal strucutre of a MATα2 homeodomain - Operator complex suggests a general model for homeodomain - DNA interactions
    • Wolberger C, Vershon AK, Liu B, Johnson AD, Pabo CO. Crystal strucutre of a MATα2 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
  • 8
    • 0027787519 scopus 로고
    • Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain - DNA complex
    • Billeter M, Qian YQ, Otting G, Müller M, Gehring W, Wüthrich K. Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain - DNA complex. J Mol Biol. 234:1993;1084-1093.
    • (1993) J Mol Biol , vol.234 , pp. 1084-1093
    • Billeter, M.1    Qian, Y.Q.2    Otting, G.3    Müller, M.4    Gehring, W.5    Wüthrich, K.6
  • 9
    • 0028263374 scopus 로고
    • Nuclear magnetic resonance solution structure of the Fushi Tarazu homeodomain from Drosophila and comparison with the Antennapedia homeodomain
    • Qian YQ, Furukobo-Tokunaga K, Resnedez-Perez D, Müller M, Gehring W, Wüthrich K. Nuclear magnetic resonance solution structure of the Fushi Tarazu homeodomain from Drosophila and comparison with the Antennapedia homeodomain. J Mol Biol. 238:1994;333-345.
    • (1994) J Mol Biol , vol.238 , pp. 333-345
    • Qian, Y.Q.1    Furukobo-Tokunaga, K.2    Resnedez-Perez, D.3    Müller, M.4    Gehring, W.5    Wüthrich, K.6
  • 10
    • 0028200262 scopus 로고
    • Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
    • Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO. 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
  • 11
    • 0029160486 scopus 로고
    • High resolution crystal structure of a paired [Pax] class cooperative homeodomain dimer on DNA
    • of outstanding interest. The co-crystal structure of the Prd HD bound to DNA provides the first example of low HD proteins interact to bind DNA cooperatively. The HDs bind to partially overlapping sites on either side of the DNA and produce a 20° bend which brings the monomers close together. The dimer interface occurs through contacts made by the amino-terminal arm of one HD with the loop between helices 2 and 3 of the other HD.
    • Wilson DS, Guenther B, Desplan C, Kuriyan J. High resolution crystal structure of a paired [Pax] class cooperative homeodomain dimer on DNA. of outstanding interest Cell. 82:1995;709-719 The co-crystal structure of the Prd HD bound to DNA provides the first example of low HD proteins interact to bind DNA cooperatively. The HDs bind to partially overlapping sites on either side of the DNA and produce a 20° bend which brings the monomers close together. The dimer interface occurs through contacts made by the amino-terminal arm of one HD with the loop between helices 2 and 3 of the other HD.
    • (1995) Cell , vol.82 , pp. 709-719
    • Wilson, D.S.1    Guenther, B.2    Desplan, C.3    Kuriyan, J.4
  • 12
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MATα2 homeodomain heterodimer bound to DNA
    • of outstanding interest. The co-crystal structure of the yeast a1 and α2 HDs bound to a 21 bp site provides the first example of how different HD proteins interact to bind DNA cooperatively. There are no direct contacts between the HDs, and all protein interactions are mediated through a helix in the α2 carboxy-terminal tail which extends from the HD and packs against helices 1 and 2 of the a1 HD to form a three-helix bundle. The proteins interact through a series of hydrogen bonds and hydrophobic contacts and it was shown that substitutions of leucine residues involved in the hydrophobic interactions appear to destroy interactions between the proteins. Binding by the a1/α2 complex produces a 60° bend that is localized in the a1 half site and between the a1 and α2 binding sites.
    • Li T, Stark MR, Johnson AD, Wolberger C. Crystal structure of the MATa1/MATα2 homeodomain heterodimer bound to DNA. of outstanding interest Science. 270:1995;262-269 The co-crystal structure of the yeast a1 and α2 HDs bound to a 21 bp site provides the first example of how different HD proteins interact to bind DNA cooperatively. There are no direct contacts between the HDs, and all protein interactions are mediated through a helix in the α2 carboxy-terminal tail which extends from the HD and packs against helices 1 and 2 of the a1 HD to form a three-helix bundle. The proteins interact through a series of hydrogen bonds and hydrophobic contacts and it was shown that substitutions of leucine residues involved in the hydrophobic interactions appear to destroy interactions between the proteins. Binding by the a1/α2 complex produces a 60° bend that is localized in the a1 half site and between the a1 and α2 binding sites.
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 13
    • 0029595248 scopus 로고
    • Structure of the even-skipped homeodomain complexed to AT-rich DNA: New perspectives on homeodomain specificity
    • of special interest. A high resolution structure of two Eve HDs bound to a 10 bp site shows that each monomer binds to opposite faces of the DNA. The structure shows that Gln50, a residue that is important for determining sequence specificity in other HD proteins, adopts several different positions and that there are several water-mediated hydrogen bonds at the protein - DNA interface.
    • Hirsch JA, Aggarwal AK. Structure of the even-skipped homeodomain complexed to AT-rich DNA: new perspectives on homeodomain specificity. of special interest EMBO J. 14:1995;6280-6291 A high resolution structure of two Eve HDs bound to a 10 bp site shows that each monomer binds to opposite faces of the DNA. The structure shows that Gln50, a residue that is important for determining sequence specificity in other HD proteins, adopts several different positions and that there are several water-mediated hydrogen bonds at the protein - DNA interface.
    • (1995) EMBO J , vol.14 , pp. 6280-6291
    • Hirsch, J.A.1    Aggarwal, A.K.2
  • 14
    • 0027936793 scopus 로고
    • The degree of variation in DNA sequence recognition among four Drosophila homeotic proteins
    • Ekker SC, Jackson DG, Von Kessler DP, Sun BI, Young KE, Beachy PA. The degree of variation in DNA sequence recognition among four Drosophila homeotic proteins. EMBO J. 13:1994;3551-3560.
    • (1994) EMBO J , vol.13 , pp. 3551-3560
    • Ekker, S.C.1    Jackson, D.G.2    Von Kessler, D.P.3    Sun, B.I.4    Young, K.E.5    Beachy, P.A.6
  • 15
    • 0028919759 scopus 로고
    • Crystal structure of a Paired domain - DNA complex at 2.5 Å reveals structural basis for Pax developmental mutations
    • Xu W, Rould MA, Jun S, Desplan C, Pabo CO. Crystal structure of a Paired domain - DNA complex at 2.5 Å reveals structural basis for Pax developmental mutations. Cell. 80:1995;639-650.
    • (1995) Cell , vol.80 , pp. 639-650
    • Xu, W.1    Rould, M.A.2    Jun, S.3    Desplan, C.4    Pabo, C.O.5
  • 16
    • 0025602459 scopus 로고
    • What determines the specificity of action of Drosophila homeodomain proteins?
    • Hayashi S, Scott MP. What determines the specificity of action of Drosophila homeodomain proteins? Cell. 63:1990;883-894.
    • (1990) Cell , vol.63 , pp. 883-894
    • Hayashi, S.1    Scott, M.P.2
  • 17
    • 0001294043 scopus 로고
    • A combinatorial regulatory circuit in budding yeast
    • K. Yamamoto, McKnight S. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Johnson AD. A combinatorial regulatory circuit in budding yeast. Yamamoto K, McKnight S. Transcriptional Regulation. 1992;975-1006 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1992) Transcriptional Regulation , pp. 975-1006
    • Johnson, A.D.1
  • 18
    • 0029124988 scopus 로고
    • The POU domain: Versatility in transcriptional regulation by a flexible two-in-one DNA binding domain
    • Herr W, Cleary MA. The POU domain: versatility in transcriptional regulation by a flexible two-in-one DNA binding domain. Genes Dev. 9:1995;1679-1693.
    • (1995) Genes Dev , vol.9 , pp. 1679-1693
    • Herr, W.1    Cleary, M.A.2
  • 19
    • 0027420571 scopus 로고
    • The Swi5 zinc-finger and Grf10 HD proteins bind DNA cooperatively at the yeast HO promoter
    • Brazas RM, Stillman DJ. The Swi5 zinc-finger and Grf10 HD proteins bind DNA cooperatively at the yeast HO promoter. Proc Natl Acad Sci USA. 90:1993;11237-11241.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11237-11241
    • Brazas, R.M.1    Stillman, D.J.2
  • 20
    • 0027966927 scopus 로고
    • The DNA binding specificity of ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein
    • Chan S, Jaffe L, Capovilla M, Botas J, Mann RS. The DNA binding specificity of ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein. Cell. 78:1994;603-615.
    • (1994) Cell , vol.78 , pp. 603-615
    • Chan, S.1    Jaffe, L.2    Capovilla, M.3    Botas, J.4    Mann, R.S.5
  • 21
    • 0028169993 scopus 로고
    • Extradenticle raises the DNA binding specificity of homeotic selector gene products
    • Van Dijk MA, Murre C. Extradenticle raises the DNA binding specificity of homeotic selector gene products. Cell. 78:1994;617-624.
    • (1994) Cell , vol.78 , pp. 617-624
    • Van Dijk, M.A.1    Murre, C.2
  • 22
    • 0027332476 scopus 로고
    • Cooperative dimerization of paired class homeodomains on DNA
    • Wilson D, Sheng G, Lecuit T, Dostatni N, Desplan C. Cooperative dimerization of paired class homeodomains on DNA. Genes Dev. 7:1993;2120-2134.
    • (1993) Genes Dev , vol.7 , pp. 2120-2134
    • Wilson, D.1    Sheng, G.2    Lecuit, T.3    Dostatni, N.4    Desplan, C.5
  • 23
    • 0028790477 scopus 로고
    • Altered DNA recognition and bending by insertions in the α2 tail of the yeast a1α2 homeodomain heterodimer
    • of outstanding interest. Base pair insertions or deletions between the a1 and α2 binding sites destroy a1/α2 cooperative binding in vitro and repression in vivo. The effects of these mutations are suppressed by the addition of residues in α2 that extend the distance between the HD and the short helix that interacts with a1. These insertions also significantly reduce the degree of DNA bending, indicating that at least one component of the bend was due to tethering the two domains together. The reduced bending does not have an effect on repression.
    • Jin Y, Mead J, Li T, Wolberger C, Vershon AK. Altered DNA recognition and bending by insertions in the α2 tail of the yeast a1α2 homeodomain heterodimer. of outstanding interest Science. 270:1995;290-293 Base pair insertions or deletions between the a1 and α2 binding sites destroy a1/α2 cooperative binding in vitro and repression in vivo. The effects of these mutations are suppressed by the addition of residues in α2 that extend the distance between the HD and the short helix that interacts with a1. These insertions also significantly reduce the degree of DNA bending, indicating that at least one component of the bend was due to tethering the two domains together. The reduced bending does not have an effect on repression.
    • (1995) Science , vol.270 , pp. 290-293
    • Jin, Y.1    Mead, J.2    Li, T.3    Wolberger, C.4    Vershon, A.K.5
  • 24
    • 0029664658 scopus 로고    scopus 로고
    • The yeast α2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes
    • of special interest. Alanine substitutions determined that a small hydrophobic patch at the amino terminus of the α2 HD was required for interaction with Mcm1 in the presence and absence of DNA. This patch bears some resemblance to the conserved hexapeptide motif found in Hox proteins, and swap experiments indicate that this motif can partially function in the context of α2. The relative positions of the α2 and Mcm1 sites are constrained and unlike the interaction with a1, are not dependent on the position of the hydrophobic patch with respect to the HD.
    • Mead J, Zhong H, Acton TB, Vershon AK. The yeast α2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes. of special interest Mol Cell Biol. 16:1996;2135-2143 Alanine substitutions determined that a small hydrophobic patch at the amino terminus of the α2 HD was required for interaction with Mcm1 in the presence and absence of DNA. This patch bears some resemblance to the conserved hexapeptide motif found in Hox proteins, and swap experiments indicate that this motif can partially function in the context of α2. The relative positions of the α2 and Mcm1 sites are constrained and unlike the interaction with a1, are not dependent on the position of the hydrophobic patch with respect to the HD.
    • (1996) Mol Cell Biol , vol.16 , pp. 2135-2143
    • Mead, J.1    Zhong, H.2    Acton, T.B.3    Vershon, A.K.4
  • 25
    • 0029102041 scopus 로고
    • Structure of serum response factor core bound to DNA
    • of outstanding interest. The co-crystal structure of the human SRF factor bound to DNA is the first example of a structure of a MADS domain bound to DNA. The structure reveals how this protein makes contacts with the DNA to produce an 80° bend. The structure also provides a framework indicating how several HD proteins may contact and bind DNA cooperatively with MADS domain proteins.
    • Pellegrini L, Tan S, Richmond TJ. Structure of serum response factor core bound to DNA. of outstanding interest Nature. 376:1995;490-498 The co-crystal structure of the human SRF factor bound to DNA is the first example of a structure of a MADS domain bound to DNA. The structure reveals how this protein makes contacts with the DNA to produce an 80° bend. The structure also provides a framework indicating how several HD proteins may contact and bind DNA cooperatively with MADS domain proteins.
    • (1995) Nature , vol.376 , pp. 490-498
    • Pellegrini, L.1    Tan, S.2    Richmond, T.J.3
  • 26
    • 0027509952 scopus 로고
    • A short, disordered protein region mediates interactions between the homeodomain of the yeast α2 protein and the MCM1 protein
    • Vershon AK, Johnson AD. A short, disordered protein region mediates interactions between the homeodomain of the yeast α2 protein and the MCM1 protein. Cell. 72:1993;105-112.
    • (1993) Cell , vol.72 , pp. 105-112
    • Vershon, A.K.1    Johnson, A.D.2
  • 27
    • 0028329225 scopus 로고
    • MCM1 point mutants deficient in expression of a-specific genes: Residues important for interaction with a1
    • Bruhn L, Sprague GF. MCM1 point mutants deficient in expression of a-specific genes: residues important for interaction with a1. Mol Cell Biol. 14:1994;2534-2544.
    • (1994) Mol Cell Biol , vol.14 , pp. 2534-2544
    • Bruhn, L.1    Sprague, G.F.2
  • 28
    • 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
    • Knoeffler P, Kamps MP. 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. 15:1995;5811-5819.
    • (1995) Mol Cell Biol , vol.15 , pp. 5811-5819
    • Knoeffler, P.1    Kamps, M.P.2
  • 29
    • 0029008293 scopus 로고
    • Cooperative interactions between HOX and PBX proteins mediated by a conserved peptide motif
    • Phelan ML, Rambaldi I, Featherstone MS. Cooperative interactions between HOX and PBX proteins mediated by a conserved peptide motif. Mol Cell Biol. 15:1995;3989-3997.
    • (1995) Mol Cell Biol , vol.15 , pp. 3989-3997
    • Phelan, M.L.1    Rambaldi, I.2    Featherstone, M.S.3
  • 30
    • 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 FB, Parker E, Krasnow MA. 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. 92:1995;739-743.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 739-743
    • Johnson, F.B.1    Parker, E.2    Krasnow, M.A.3
  • 31
    • 0028947525 scopus 로고
    • Pbx proteins display hexapeptide-dependent cooperative DNA binding with a subset of Hox proteins
    • Chang C-P, Shen W-F, Rozenfeld S, Lawrence HJ, Largman C, Cleary ML. Pbx proteins display hexapeptide-dependent cooperative DNA binding with a subset of Hox proteins. Genes Dev. 9:1995;663-674.
    • (1995) Genes Dev , vol.9 , pp. 663-674
    • Chang C-P1    Shen W-F2    Rozenfeld, S.3    Lawrence, H.J.4    Largman, C.5    Cleary, M.L.6
  • 32
    • 0029079663 scopus 로고
    • The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins
    • Neuteboom STC, Peltenburg LTC, Van Dijk MA, Murre C. The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins. Proc Natl Acad Sci USA. 92:1995;9166-9170.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9166-9170
    • Neuteboom, S.T.C.1    Peltenburg, L.T.C.2    Van Dijk, M.A.3    Murre, C.4
  • 33
    • 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, Scheele J, Wright DD, Kamps MP. 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. 15:1995;3786-3795.
    • (1995) Mol Cell Biol , vol.15 , pp. 3786-3795
    • Lu, Q.1    Knoepfler, P.2    Scheele, J.3    Wright, D.D.4    Kamps, M.P.5
  • 34
    • 0029939199 scopus 로고    scopus 로고
    • Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus
    • Chang CP, Brocchieri L, Shen WF, Largman C, Cleary ML. Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus. Mol Cell Biol. 16:1996;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
  • 35
    • 0029890916 scopus 로고    scopus 로고
    • A structural model for HOX-extradenticle - DNA complex accounts for the choice of HOX proteins in the heterodimer
    • Chan SK, Mann RS. A structural model for HOX-extradenticle - DNA complex accounts for the choice of HOX proteins in the heterodimer. Proc Natl Acad Sci USA. 93:1996;5223-5228.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5223-5228
    • Chan, S.K.1    Mann, R.S.2
  • 36
    • 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
    • of outstanding interest. An investigation into the sequence requirements in Pbx1 for cooperative binding with HoxA5. Experiments show that a synthetic peptide with the hexapeptide motif will inhibit cooperative interactions between HoxA5 and Pbx1, and that addition of this peptide to Pbx1 alone will increase the DNA-binding affinity of the protein, suggesting that it may stabilize the fold of the HD. Amino acid substitutions in Pbx1 showed that residues in the turn between helices 1 and 2 of the HD are required for cooperative DNA binding with HoxA5. A region carboxy-terminal to the Pbx1 HD also appears to play a role in DNA binding or stability of the complex.
    • Lu Q, Kamps MP. Structural determinants within Pbx1 that mediate cooperative DNA binding with pentapeptide-containing Hox proteins: proposal for a model of a Pbx1 - Hox - DNA complex. of outstanding interest Mol Cell Biol. 16:1996;1632-1640 An investigation into the sequence requirements in Pbx1 for cooperative binding with HoxA5. Experiments show that a synthetic peptide with the hexapeptide motif will inhibit cooperative interactions between HoxA5 and Pbx1, and that addition of this peptide to Pbx1 alone will increase the DNA-binding affinity of the protein, suggesting that it may stabilize the fold of the HD. Amino acid substitutions in Pbx1 showed that residues in the turn between helices 1 and 2 of the HD are required for cooperative DNA binding with HoxA5. A region carboxy-terminal to the Pbx1 HD also appears to play a role in DNA binding or stability of the complex.
    • (1996) Mol Cell Biol , vol.16 , pp. 1632-1640
    • Lu, Q.1    Kamps, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.