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Volumn 13, Issue 20, 1999, Pages 2650-2657

Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: Specific recognition of a protein-DNA interface

Author keywords

Crystal structure; Immunoglobulin; OCA B; Oct 1; Octamer; POU domain; Protein DNA complex; Protein DNA interface; Transcription

Indexed keywords

DNA; PEPTIDE; PEPTIDE OCA B; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0033569643     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.13.20.2650     Document Type: Article
Times cited : (81)

References (34)
  • 1
    • 0027465103 scopus 로고
    • The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain
    • Assa-Munt, N., R.J. Mortishire-Smith, R. Aurora, W. Herr, and P.E. Wright. 1993. The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain. Cell 73: 193-205.
    • (1993) Cell , vol.73 , pp. 193-205
    • Assa-Munt, N.1    Mortishire-Smith, R.J.2    Aurora, R.3    Herr, W.4    Wright, P.E.5
  • 2
    • 0030679566 scopus 로고    scopus 로고
    • OCA-B is a functional analog of VP16 but targets a separate surface of the Oct-1 POU domain
    • Babb, R., M.A. Cleary, and W. Herr. 1997. OCA-B is a functional analog of VP16 but targets a separate surface of the Oct-1 POU domain. Mol. Cell Biol. 17: 7295-7305.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 7295-7305
    • Babb, R.1    Cleary, M.A.2    Herr, W.3
  • 3
    • 0032512459 scopus 로고    scopus 로고
    • The structure of GABPalpha/beta: An ETS domain-ankyrin repeat heterodimer bound to DNA
    • Batchelor, A.H., D.E. Piper, F.C. de la Brousse, S.L. McKnight, and C. Wolberger. 1998. The structure of GABPalpha/beta: An ETS domain-ankyrin repeat heterodimer bound to DNA. Science 279: 1037-1041.
    • (1998) Science , vol.279 , pp. 1037-1041
    • Batchelor, A.H.1    Piper, D.E.2    De La Brousse, F.C.3    McKnight, S.L.4    Wolberger, C.5
  • 4
    • 0003951876 scopus 로고    scopus 로고
    • v. 3.851. Yale University, New Haven, CT
    • Brunger, A. 1996. XPLOR, v. 3.851. Yale University, New Haven, CT.
    • (1996) XPLOR
    • Brunger, A.1
  • 5
    • 0029967014 scopus 로고    scopus 로고
    • Sequence-specific DNA binding of the B-cell-specific coactivator OCA-B
    • Cepek, K.L., D.I. Chasman, and P.A. Sharp. 1996. Sequence-specific DNA binding of the B-cell-specific coactivator OCA-B. Genes & Dev. 10: 2079-2088.
    • (1996) Genes & Dev. , vol.10 , pp. 2079-2088
    • Cepek, K.L.1    Chasman, D.I.2    Sharp, P.A.3
  • 6
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA
    • Chen, F.E., D.B. Huang, Y.Q. Chen, and G. Ghosh. 1998a. Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA. Nature 391: 410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 7
    • 0032485391 scopus 로고    scopus 로고
    • Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA
    • Chen, L., J.N. Glover, P.C. Hogan, A. Rao, and S.C. Harrison. 1998b. Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA. Nature 392: 42-48.
    • (1998) Nature , vol.392 , pp. 42-48
    • Chen, L.1    Glover, J.N.2    Hogan, P.C.3    Rao, A.4    Harrison, S.C.5
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50: 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 9
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly, M.L. 1983. Solvent-accessible surfaces of proteins and nucleic acids. Science 221: 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 10
    • 0002583957 scopus 로고
    • 'dm': An automated procedure for phase improvement by density modification
    • Daresbury Laboratory, Warrington, UK
    • Cowtan, K. 1994. 'dm': An automated procedure for phase improvement by density modification. In Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31: 34-38. Daresbury Laboratory, Warrington, UK.
    • (1994) Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 12
    • 0027609916 scopus 로고
    • Setor: Hardware lighted three-dimensional model representations of macromolecules
    • Evans, S. 1993. Setor: Hardware lighted three-dimensional model representations of macromolecules. J. Mol. Graphics 11: 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.1
  • 13
    • 0032533226 scopus 로고    scopus 로고
    • The Oct-1 POU domain activates snRNA gene transcription by contacting a region in the SNAPc largest subunit that bears sequence similarities to the Oct-1 coactivator OBF-1
    • Ford, E., M. Strubin, and N. Hernandez. 1998. The Oct-1 POU domain activates snRNA gene transcription by contacting a region in the SNAPc largest subunit that bears sequence similarities to the Oct-1 coactivator OBF-1. Genes & Dev. 12: 3528-3540.
    • (1998) Genes & Dev. , vol.12 , pp. 3528-3540
    • Ford, E.1    Strubin, M.2    Hernandez, N.3
  • 14
  • 15
    • 0029935909 scopus 로고    scopus 로고
    • The B-cell coactivator Bob1 shows DNA sequence-dependent complex formation with oct-1/Oct-2 factors, leading to differential promoter activation
    • Gstaiger, M., O. Georgiev, H. van Leeuwen, P. van der Vliet, and W. Schaffner. 1996. The B-cell coactivator Bob1 shows DNA sequence-dependent complex formation with Oct-1/Oct-2 factors, leading to differential promoter activation. EMBO J. 15: 2781-2790.
    • (1996) EMBO J. , vol.15 , pp. 2781-2790
    • Gstaiger, M.1    Georgiev, O.2    Van Leeuwen, H.3    Van Der Vliet, P.4    Schaffner, W.5
  • 16
    • 0031057121 scopus 로고    scopus 로고
    • Structure of Pit-1 POU domain bound to DNA as a dimer: Unexpected arrangement and flexibility
    • Jacobson, E.M., P. Li, A. Leon-del-Rio, M.G. Rosenfeld, and A.K. Aggarwal. 1997. Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility. Genes & Dev. 11: 198-212.
    • (1997) Genes & Dev. , vol.11 , pp. 198-212
    • Jacobson, E.M.1    Li, P.2    Leon-Del-Rio, A.3    Rosenfeld, M.G.4    Aggarwal, A.K.5
  • 17
    • 0002552477 scopus 로고
    • A set of averaging programs
    • ed. E. Dodson, S. Cover, and W. Wolf, SERC Daresbury Laboratory, Warrington, UK
    • Jones, T. 1992. A set of averaging programs. In Molecular replacement (ed. E. Dodson, S. Cover, and W. Wolf), pp. 91-105. SERC Daresbury Laboratory, Warrington, UK.
    • (1992) Molecular Replacement , pp. 91-105
    • Jones, T.1
  • 18
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these
    • Jones, T.A., J.-Y. Zou, S.W. Cowan, and M. Kjelgaard. 1991. Improved methods for the building of protein models in electron density maps and the location of errors in these. Acta Crystallogr. A47: 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 19
    • 0029917392 scopus 로고    scopus 로고
    • The B-cell-specific transcription coactivator OCA-B/OBF-1/Bob-1 is essential for normal production of immunoglobulin isotypes
    • Kim, U., X.F. Qin, S. Gong, S. Stevens, Y. Luo, M. Nussenzweig, and R.G. Roeder. 1996. The B-cell-specific transcription coactivator OCA-B/OBF-1/Bob-1 is essential for normal production of immunoglobulin isotypes. Nature 383: 542-547.
    • (1996) Nature , vol.383 , pp. 542-547
    • Kim, U.1    Qin, X.F.2    Gong, S.3    Stevens, S.4    Luo, Y.5    Nussenzweig, M.6    Roeder, R.G.7
  • 20
    • 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., M.A. Rould, R. Aurora, W. Herr, and C.O. Pabo. 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
  • 21
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • ed. C. W. Carter, Jr. and R. M. Sweet, Academic Press, New York, NY
    • La Fortelle, E. and G. Bricogne. 1997. Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD Methods. In Methods in Enzymology, Macromolecular Crystallography (ed. C. W. Carter, Jr. and R. M. Sweet), pp. 472-494. Academic Press, New York, NY.
    • (1997) Methods in Enzymology, Macromolecular Crystallography , pp. 472-494
    • La Fortelle, E.1    Bricogne, G.2
  • 22
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., M.W. MacArthur, D.S. Moss, and J.M. Thornton. 1993. PROCHECK - A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA
    • Li, T., M.R. Stark, A.D. Johnson, and C. Wolberger. 1995. Crystal structure of the MATa1/MAT alpha 2 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
  • 24
    • 0029041509 scopus 로고
    • Cloning, functional characterization, and mechanism of action of the B-cell-specific transcriptional coactivator OCA-B
    • Luo, Y. and R.G. Roeder. 1995. Cloning, functional characterization, and mechanism of action of the B-cell-specific transcriptional coactivator OCA-B. Mol. Cell Biol. 15: 4115-4124.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4115-4124
    • Luo, Y.1    Roeder, R.G.2
  • 25
    • 0026693624 scopus 로고
    • A novel B-cell-derived coactivator potentiates the activation of immunoglobulin promoters by octamer-binding transcription factors
    • Luo, Y., H. Fujii, T. Gerster, and R.G. Roeder. 1992. A novel B-cell-derived coactivator potentiates the activation of immunoglobulin promoters by octamer-binding transcription factors. Cell 71: 231-241.
    • (1992) Cell , vol.71 , pp. 231-241
    • Luo, Y.1    Fujii, H.2    Gerster, T.3    Roeder, R.G.4
  • 26
    • 0031835435 scopus 로고    scopus 로고
    • Coactivation by OCA-B: Definition of critical regions and synergism with general cofactors
    • Luo, Y., H. Ge, S. Stevens, H. Xiao, and R.G. Roeder. 1998. Coactivation by OCA-B: definition of critical regions and synergism with general cofactors. Mol. Cell Biol. 18: 3803-3810.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3803-3810
    • Luo, Y.1    Ge, H.2    Stevens, S.3    Xiao, H.4    Roeder, R.G.5
  • 27
    • 0029911579 scopus 로고    scopus 로고
    • The Oct-1 POU-specific domain can stimulate small nuclear RNA gene transcription by stabilizing the basal transcription complex SNAPc
    • Mittal, V., M.A. Cleary, W. Herr, and N. Hernandez. 1996. The Oct-1 POU-specific domain can stimulate small nuclear RNA gene transcription by stabilizing the basal transcription complex SNAPc. Mol. Cell Biol. 16: 1955-1965.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1955-1965
    • Mittal, V.1    Cleary, M.A.2    Herr, W.3    Hernandez, N.4
  • 28
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr. A50: 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • ed. C.W. Carter, Jr., and R.M. Sweet, Academic Press, New York, NY
    • Otwinowski, Z. and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology, Macromolecular crystallography (ed. C.W. Carter, Jr., and R.M. Sweet), Vol. 276, pp.307-326. Academic Press, New York, NY
    • (1997) Methods in Enzymology, Macromolecular Crystallography , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. 1986. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A42: 140-149.
    • (1986) Acta Crystallogr. , vol.A42 , pp. 140-149
    • Read, R.J.1
  • 31
    • 0031784025 scopus 로고    scopus 로고
    • Coactivator OBF-1 makes selective contacts with both the POU-specific domain and the POU homeodomain and acts as a molecular clamp on DNA
    • Sauter, P. and P. Matthias. 1998. Coactivator OBF-1 makes selective contacts with both the POU-specific domain and the POU homeodomain and acts as a molecular clamp on DNA. Mol. Cell Biol. 18: 7397-7409.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 7397-7409
    • Sauter, P.1    Matthias, P.2
  • 32
    • 0029967024 scopus 로고    scopus 로고
    • B-cell-specific coactivator OBF-1/OCA-B/ Bob1 required for immune response and germinal centre formation
    • Schubart, D.B., A. Rolink, M.H. Kosco-Vilbois, F. Botteri, and P. Matthias. 1996. B-cell-specific coactivator OBF-1/OCA-B/ Bob1 required for immune response and germinal centre formation. Nature 383: 538-542.
    • (1996) Nature , vol.383 , pp. 538-542
    • Schubart, D.B.1    Rolink, A.2    Kosco-Vilbois, M.H.3    Botteri, F.4    Matthias, P.5
  • 33
    • 0028842156 scopus 로고
    • OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin promoter activity through association with octamer-binding proteins
    • Strubin, M., J.W. Newell, and P. Matthias. 1995. OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin promoter activity through association with octamer-binding proteins. Cell 80: 497-506.
    • (1995) Cell , vol.80 , pp. 497-506
    • Strubin, M.1    Newell, J.W.2    Matthias, P.3
  • 34
    • 0032509980 scopus 로고    scopus 로고
    • Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex
    • Tan, S. and T.J. Richmond. 1998. Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex. Nature 391: 660-666.
    • (1998) Nature , vol.391 , pp. 660-666
    • Tan, S.1    Richmond, T.J.2


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