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Volumn 10, Issue 6, 2001, Pages 1244-1253

The HoxB1 hexapeptide is a prefolded domain: Implications for the Pbx 1/Hox interaction

Author keywords

DNA; Hox; Inhibitor; NMR; Pbx; Peptide; Transcription

Indexed keywords

HEXAPEPTIDE; HOMEODOMAIN PROTEIN;

EID: 0035019657     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.50901     Document Type: Article
Times cited : (27)

References (35)
  • 1
    • 0023635756 scopus 로고
    • The molecular basis for metameric pattern in the Drosophila embryo
    • Akam, M., 1987. The molecular basis for metameric pattern in the Drosophila embryo. Development 101: 1-22.
    • (1987) Development , vol.101 , pp. 1-22
    • Akam, M.1
  • 2
    • 0030858227 scopus 로고    scopus 로고
    • Extracting information from the temperature gradients of polypeptide NH chemical shifts. I. The importance of conformational averaging
    • Andersen, N.H., Neidigh, J.W., Harris, S.M., Lee, G.M., Liu, Z., and Tong, H. 1997. Extracting information from the temperature gradients of polypeptide NH chemical shifts. I. The importance of conformational averaging. J. Am. Chem. Soc. 119: 8547-8561.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8547-8561
    • Andersen, N.H.1    Neidigh, J.W.2    Harris, S.M.3    Lee, G.M.4    Liu, Z.5    Tong, H.6
  • 3
    • 0029558541 scopus 로고
    • A novel homeobox protein which recognizes a TGT core and functionally interferes with a retinoid-responsive motif
    • Bertolino, E., Reimund, B., Wildt-Perinic, D., and Clerc, R.G. 1995. A novel homeobox protein which recognizes a TGT core and functionally interferes with a retinoid-responsive motif. J. Biol. Chem. 270: 31178-31188.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31178-31188
    • Bertolino, E.1    Reimund, B.2    Wildt-Perinic, D.3    Clerc, R.G.4
  • 6
    • 0033986595 scopus 로고    scopus 로고
    • May the driving force be with you - Whatever it is
    • Cavanagh, J. and Akke, M. 2000. May the driving force be with you - Whatever it is. Nat. Struct. Biol. 7: 11-13.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 11-13
    • Cavanagh, J.1    Akke, M.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
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution I. Sequence requirements for the formation of a reverse turn
    • Dyson, H.J., Rance, M., Houghten, A., Lerner, R.A., and Wright, P.E. 1988. Folding of immunogenic peptide fragments of proteins in water solution I. Sequence requirements for the formation of a reverse turn. J. Mol. Biol. 201: 161-200.
    • (1988) J. Mol. Biol. , vol.201 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghten, A.3    Lerner, R.A.4    Wright, P.E.5
  • 9
    • 0032756923 scopus 로고    scopus 로고
    • The 'dynamics' in the thermodynamics of binding
    • Forman-Kay, J. 1999. The 'Dynamics' in the thermodynamics of binding. Nat. Struct. Biol. 6: 1086-1087.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1086-1087
    • Forman-Kay, J.1
  • 11
    • 0025894715 scopus 로고
    • Deregulation of a homdobox gene, HOX11 by the t(10;14) in T cell leukemia
    • Hatano, M., Roberts, C.W., Minden, M., Crist, W.M., and Korsmeyer, S.J. 1991. Deregulation of a homdobox gene, HOX11 by the t(10;14) in T cell leukemia. Science 253: 79-82.
    • (1991) Science , vol.253 , pp. 79-82
    • Hatano, M.1    Roberts, C.W.2    Minden, M.3    Crist, W.M.4    Korsmeyer, S.J.5
  • 12
    • 0033588116 scopus 로고    scopus 로고
    • NMR studies of the Pbs1 TALE homeodomain protein free in solution and bound to DNA: Proposal for a mechanism of Hoxb1 - Pbx1 - DNA complex assembly
    • Jabet, C., Gitti, R., Summers, M.F., and Wolberger, C. 1999. NMR studies of the Pbs1 TALE homeodomain protein free in solution and bound to DNA: Proposal for a mechanism of HoxB1 - Pbx1 - DNA complex assembly. J. Mol. Biol. 291: 521-530.
    • (1999) J. Mol. Biol. , vol.291 , pp. 521-530
    • Jabet, C.1    Gitti, R.2    Summers, M.F.3    Wolberger, C.4
  • 13
    • 34249765651 scopus 로고
    • NMR view: A computer program for the visualization and analysis of NMR data
    • Johnson, B.A. and Blevins, R.A. 1994. NMR View: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4: 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 14
    • 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.H., 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.H.3    Baltimore, D.4
  • 15
    • 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. 15: 5811-5819.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5811-5819
    • Knoepfler, P.S.1    Kamps, M.P.2
  • 16
    • 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
  • 17
    • 0033997037 scopus 로고    scopus 로고
    • Structure-based thermodynamic analysis of the dissociation of protein - Phosphatase - 1 catalytic subunit and microcystin - LR docked complexes
    • Lavigne, P., Bagu, J.R., Boyko, R., Willard, L., Holmes, C.F.B., and Sykes, B.D. 2000. Structure-based thermodynamic analysis of the dissociation of protein - phosphatase - 1 catalytic subunit and microcystin - LR docked complexes. Protein Sci. 9: 252-264.
    • (2000) Protein Sci. , vol.9 , pp. 252-264
    • Lavigne, P.1    Bagu, J.R.2    Boyko, R.3    Willard, L.4    Holmes, C.F.B.5    Sykes, B.D.6
  • 18
    • 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
  • 19
    • 0029898760 scopus 로고    scopus 로고
    • Extra specificity from extradenticle: The partnership between HOX and PBX/EXD homeodomain proteins
    • Mann, R.S. and Chan, S.K. 1996. Extra specificity from extradenticle: the partnership between HOX and PBX/EXD homeodomain proteins. Trends Genet. 12: 258-262.
    • (1996) Trends Genet. , vol.12 , pp. 258-262
    • Mann, R.S.1    Chan, S.K.2
  • 20
    • 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
  • 21
    • 0029207339 scopus 로고
    • 'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • Mertuka, G., Dyson, H.J., and Wright, P.E. 1995. 'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR 5: 14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Mertuka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 23
    • 0033933054 scopus 로고    scopus 로고
    • The cisproline(i -1) - Aromatic(i) interaction: Folding of the Ala - CisPro - Tyr peptide characterized by NMR and theoretical approaches
    • Nardi, R, Kemmink, J., Sattler, M., and Wade, R.C. 2000. The cisproline(i -1) - aromatic(i) interaction: Folding of the Ala - cisPro - Tyr peptide characterized by NMR and theoretical approaches. J. Biomol. NMR 17: 63-77.
    • (2000) J. Biomol. NMR , vol.17 , pp. 63-77
    • Nardi, R.1    Kemmink, J.2    Sattler, M.3    Wade, R.C.4
  • 24
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry - Dynamical simulated annealing calculations
    • Nilges, M., Clore, G.M., and Gronenborn, A.M. 1988. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry - dynamical simulated annealing calculations. Febs Lett. 229:317-324.
    • (1988) Febs Lett. , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 25
    • 0025064238 scopus 로고
    • Chromosomal translocation t(1;19) results in synthesis of a homeobox 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 homeobox 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
  • 26
    • 0033602242 scopus 로고    scopus 로고
    • Structure of a DNA - Bound ultrabithorax - Extradenticle homeodomain complex
    • Passner, J.M., Ryoo, H.D., Shen, L., Mann, R.S., and Aggarwal, A.K. 1999. Structure of a DNA - bound Ultrabithorax - Extradenticle homeodomain complex. Nature 397: 714-719.
    • (1999) Nature , vol.397 , pp. 714-719
    • Passner, J.M.1    Ryoo, H.D.2    Shen, L.3    Mann, R.S.4    Aggarwal, A.K.5
  • 27
    • 0033582545 scopus 로고    scopus 로고
    • Structure of a HoxB1 - Pbx1 heterodimer bound to DNA: Role of the hexapeptide and a fourth homeodomain helix in complex formation
    • Piper, D.E., Batchelor, A.H., Chang, C.P., Cleary, M.L., and Wolberger, C. 1999. Structure of a HoxB1 - Pbx1 heterodimer bound to DNA: Role of the hexapeptide and a fourth homeodomain helix in complex formation. Cell 96: 587-597.
    • (1999) Cell , vol.96 , pp. 587-597
    • Piper, D.E.1    Batchelor, A.H.2    Chang, C.P.3    Cleary, M.L.4    Wolberger, C.5
  • 31
    • 0028169993 scopus 로고
    • Extradenticle raises the DNA binding specificity of homeotic selector gene products
    • van Dijk, M.A. and Murre, C. 1994. Extradenticle raises the DNA binding specificity of homeotic selector gene products. Cell 78: 617-624.
    • (1994) Cell , vol.78 , pp. 617-624
    • Van Dijk, M.A.1    Murre, C.2
  • 32
    • 0025113022 scopus 로고
    • b-turns and their distortions: A proposed new nomenclature
    • Wilmot, C.M. and Thornton, J.M. 1990. b-Turns and their distortions: a proposed new nomenclature. Prot. Eng. 3: 479-493.
    • (1990) Prot. Eng. , vol.3 , pp. 479-493
    • Wilmot, C.M.1    Thornton, J.M.2
  • 33
    • 0033111987 scopus 로고    scopus 로고
    • Structural basis of hox specificity
    • Wilson, D.S. and Desplan, C. 1999. Structural basis of Hox specificity. Nat. Struct. Biol. 6: 297-300.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 297-300
    • Wilson, D.S.1    Desplan, C.2
  • 34
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5: 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5


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