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Volumn 370, Issue 5, 2007, Pages 826-836

Cyclin Box Structure of the P-TEFb Subunit Cyclin T1 Derived from a Fusion Complex with EIAV Tat

Author keywords

crystal structure; cyclin T1; P TEFb; Tat; transcription

Indexed keywords

CYCLIN DEPENDENT KINASE 9; CYCLIN T1; HYBRID PROTEIN; POSITIVE TRANSCRIPTION ELONGATION FACTOR B;

EID: 34250196457     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.077     Document Type: Article
Times cited : (36)

References (54)
  • 1
    • 0028290825 scopus 로고
    • Control of RNA initiation and elongation at the HIV-1 promoter
    • Jones K.A., and Peterlin B.M. Control of RNA initiation and elongation at the HIV-1 promoter. Annu. Rev. Biochem. 63 (1994) 717-743
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 717-743
    • Jones, K.A.1    Peterlin, B.M.2
  • 2
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei P., Garber M.E., Fang S.M., Fischer W.H., and Jones K.A. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 92 (1998) 451-462
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.M.3    Fischer, W.H.4    Jones, K.A.5
  • 3
    • 0032533253 scopus 로고    scopus 로고
    • The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein
    • Garber M.E., Wei P., Kewal Ramani V.N., Mayall T. P., Herrmann C.H., and Rice A.P. The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein. Genes Dev. 12 (1998) 3512-3527
    • (1998) Genes Dev. , vol.12 , pp. 3512-3527
    • Garber, M.E.1    Wei, P.2    Kewal Ramani, V.N.3    Mayall, T. P.4    Herrmann, C.H.5    Rice, A.P.6
  • 4
    • 0842324788 scopus 로고    scopus 로고
    • Recycling the cell cycle: cyclins revisited
    • Murray A.W. Recycling the cell cycle: cyclins revisited. Cell 116 (2004) 221-234
    • (2004) Cell , vol.116 , pp. 221-234
    • Murray, A.W.1
  • 7
    • 33746403681 scopus 로고    scopus 로고
    • Controlling the elongation phase of transcription with P-TEFb
    • Peterlin B.M., and Price D.H. Controlling the elongation phase of transcription with P-TEFb. Mol. Cell 23 (2006) 297-305
    • (2006) Mol. Cell , vol.23 , pp. 297-305
    • Peterlin, B.M.1    Price, D.H.2
  • 9
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo A.A., Jeffrey P.D., Patten A.K., Massague J., and Pavletich N.P. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382 (1996) 325-331
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5
  • 10
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown N.R., Noble M.E., Endicott J.A., and Johnson L.N. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nature Cell Biol. 1 (1999) 438-443
    • (1999) Nature Cell Biol. , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.2    Endicott, J.A.3    Johnson, L.N.4
  • 11
    • 0036176979 scopus 로고    scopus 로고
    • Structural basis for CDK6 activation by a virus-encoded cyclin
    • Schulze-Gahmen U., and Kim S.H. Structural basis for CDK6 activation by a virus-encoded cyclin. Nature Struct. Biol. 9 (2002) 177-181
    • (2002) Nature Struct. Biol. , vol.9 , pp. 177-181
    • Schulze-Gahmen, U.1    Kim, S.H.2
  • 12
    • 14844307019 scopus 로고    scopus 로고
    • The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles
    • Honda R., Lowe E.D., Dubinina E., Skamnaki V., Cook A., Brown N.R., and Johnson L.N. The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles. EMBO J. 24 (2005) 452-463
    • (2005) EMBO J. , vol.24 , pp. 452-463
    • Honda, R.1    Lowe, E.D.2    Dubinina, E.3    Skamnaki, V.4    Cook, A.5    Brown, N.R.6    Johnson, L.N.7
  • 14
    • 0032031706 scopus 로고    scopus 로고
    • Identification of multiple cyclin subunits of human P-TEFb
    • Peng J., Zhu Y., Milton J.T., and Price D.H. Identification of multiple cyclin subunits of human P-TEFb. Genes Dev. 12 (1998) 755-762
    • (1998) Genes Dev. , vol.12 , pp. 755-762
    • Peng, J.1    Zhu, Y.2    Milton, J.T.3    Price, D.H.4
  • 16
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall N.F., Peng J., Xie Z., and Price D.H. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271 (1996) 27176-27183
    • (1996) J. Biol. Chem. , vol.271 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, Z.3    Price, D.H.4
  • 17
    • 0032534814 scopus 로고    scopus 로고
    • Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro
    • Wada T., Takagi T., Yamaguchi Y., Watanabe D., and Handa H. Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J. 17 (1998) 7395-7403
    • (1998) EMBO J. , vol.17 , pp. 7395-7403
    • Wada, T.1    Takagi, T.2    Yamaguchi, Y.3    Watanabe, D.4    Handa, H.5
  • 18
    • 0042592926 scopus 로고    scopus 로고
    • CDK9 is constitutively expressed throughout the cell cycle, and its steady-state expression is independent of SKP2
    • Garriga J., Bhattacharya S., Calbo J., Marshall R.M., Truongcao M., Haines D.S., and Grana X. CDK9 is constitutively expressed throughout the cell cycle, and its steady-state expression is independent of SKP2. Mol. Cell. Biol. 23 (2003) 5165-5173
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5165-5173
    • Garriga, J.1    Bhattacharya, S.2    Calbo, J.3    Marshall, R.M.4    Truongcao, M.5    Haines, D.S.6    Grana, X.7
  • 19
    • 0038111978 scopus 로고    scopus 로고
    • MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner
    • Michels A.A., Nguyen V.T., Fraldi A., Labas V., Edwards M., Bonnet F., et al. MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a transcription-dependent manner. Mol. Cell. Biol. 23 (2003) 4859-4869
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4859-4869
    • Michels, A.A.1    Nguyen, V.T.2    Fraldi, A.3    Labas, V.4    Edwards, M.5    Bonnet, F.6
  • 20
    • 0242361319 scopus 로고    scopus 로고
    • Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA
    • Yik J.H., Chen R., Nishimura R., Jennings J.L., Link A.J., and Zhou Q. Inhibition of P-TEFb (CDK9/Cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA. Mol. Cell 12 (2003) 971-982
    • (2003) Mol. Cell , vol.12 , pp. 971-982
    • Yik, J.H.1    Chen, R.2    Nishimura, R.3    Jennings, J.L.4    Link, A.J.5    Zhou, Q.6
  • 21
    • 0036851825 scopus 로고    scopus 로고
    • Activation and function of cyclin T-Cdk9 (positive transcription elongation factor-b) in cardiac muscle-cell hypertrophy
    • Sano M., Abdellatif M., Oh H., Xie M., Bagella L., Giordano A., et al. Activation and function of cyclin T-Cdk9 (positive transcription elongation factor-b) in cardiac muscle-cell hypertrophy. Nature Med. 8 (2002) 1310-1317
    • (2002) Nature Med. , vol.8 , pp. 1310-1317
    • Sano, M.1    Abdellatif, M.2    Oh, H.3    Xie, M.4    Bagella, L.5    Giordano, A.6
  • 22
    • 24644486087 scopus 로고    scopus 로고
    • The breast cell growth inhibitor, estrogen down regulated gene 1, modulates a novel functional interaction between estrogen receptor alpha and transcriptional elongation factor cyclin T1
    • Wittmann B.M., Fujinaga K., Deng H., Ogba N., and Montano M.M. The breast cell growth inhibitor, estrogen down regulated gene 1, modulates a novel functional interaction between estrogen receptor alpha and transcriptional elongation factor cyclin T1. Oncogene 24 (2005) 5576-5588
    • (2005) Oncogene , vol.24 , pp. 5576-5588
    • Wittmann, B.M.1    Fujinaga, K.2    Deng, H.3    Ogba, N.4    Montano, M.M.5
  • 23
    • 0032701796 scopus 로고    scopus 로고
    • Tackling Tat
    • Karn J. Tackling Tat. J. Mol. Biol. 293 (1999) 235-254
    • (1999) J. Mol. Biol. , vol.293 , pp. 235-254
    • Karn, J.1
  • 24
    • 0033604520 scopus 로고    scopus 로고
    • Tat transactivation: a model for the regulation of eukaryotic transcriptional elongation
    • Taube R., Fujinaga K., Wimmer J., Barboric M., and Peterlin B.M. Tat transactivation: a model for the regulation of eukaryotic transcriptional elongation. Virology 264 (1999) 245-253
    • (1999) Virology , vol.264 , pp. 245-253
    • Taube, R.1    Fujinaga, K.2    Wimmer, J.3    Barboric, M.4    Peterlin, B.M.5
  • 27
    • 0033986157 scopus 로고    scopus 로고
    • Interactions between equine cyclin T1, Tat, and TAR are disrupted by a leucine-to-valine substitution found in human cyclin T1
    • Taube R., Fujinaga K., Irwin D., Wimmer J., Geyer M., and Peterlin B.M. Interactions between equine cyclin T1, Tat, and TAR are disrupted by a leucine-to-valine substitution found in human cyclin T1. J. Virol. 74 (2000) 892-898
    • (2000) J. Virol. , vol.74 , pp. 892-898
    • Taube, R.1    Fujinaga, K.2    Irwin, D.3    Wimmer, J.4    Geyer, M.5    Peterlin, B.M.6
  • 28
    • 0034009884 scopus 로고    scopus 로고
    • Canine cyclin T1 rescues equine infectious anemia virus tat trans-activation in human cells
    • Albrecht T.R., Lund L.H., and Garcia-Blanco M.A. Canine cyclin T1 rescues equine infectious anemia virus tat trans-activation in human cells. Virology 268 (2000) 7-11
    • (2000) Virology , vol.268 , pp. 7-11
    • Albrecht, T.R.1    Lund, L.H.2    Garcia-Blanco, M.A.3
  • 29
    • 0036891860 scopus 로고    scopus 로고
    • A minimal chimera of human cyclin T1 and Tat binds TAR and activates human immunodeficiency virus transcription in murine cells
    • Fujinaga K., Irwin D., Taube R., Zhang F., Geyer M., and Peterlin B.M. A minimal chimera of human cyclin T1 and Tat binds TAR and activates human immunodeficiency virus transcription in murine cells. J. Virol. 76 (2002) 12934-12939
    • (2002) J. Virol. , vol.76 , pp. 12934-12939
    • Fujinaga, K.1    Irwin, D.2    Taube, R.3    Zhang, F.4    Geyer, M.5    Peterlin, B.M.6
  • 30
    • 0031055890 scopus 로고    scopus 로고
    • The structure of cyclin H: common mode of kinase activation and specific features
    • Andersen G., Busso D., Poterszman A., Hwang J.R., Wurtz J.M., Ripp R., et al. The structure of cyclin H: common mode of kinase activation and specific features. EMBO J. 16 (1997) 958-967
    • (1997) EMBO J. , vol.16 , pp. 958-967
    • Andersen, G.1    Busso, D.2    Poterszman, A.3    Hwang, J.R.4    Wurtz, J.M.5    Ripp, R.6
  • 31
    • 0030694039 scopus 로고    scopus 로고
    • The cyclin box fold: protein recognition in cell-cycle and transcription control
    • Noble M.E., Endicott J.A., Brown N.R., and Johnson L.N. The cyclin box fold: protein recognition in cell-cycle and transcription control. Trends Biochem. Sci. 22 (1997) 482-487
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 482-487
    • Noble, M.E.1    Endicott, J.A.2    Brown, N.R.3    Johnson, L.N.4
  • 32
    • 21944438071 scopus 로고    scopus 로고
    • Structure of the mediator subunit cyclin C and its implications for CDK8 function
    • Hoeppner S., Baumli S., and Cramer P. Structure of the mediator subunit cyclin C and its implications for CDK8 function. J. Mol. Biol. 350 (2005) 833-842
    • (2005) J. Mol. Biol. , vol.350 , pp. 833-842
    • Hoeppner, S.1    Baumli, S.2    Cramer, P.3
  • 33
    • 33846483298 scopus 로고    scopus 로고
    • Crystal structure of human Cyclin K, a positive regulator of cyclin-dependent kinase 9
    • Baek K., Brown R.S., Birrane G., and Ladias J.A. Crystal structure of human Cyclin K, a positive regulator of cyclin-dependent kinase 9. J. Mol. Biol. 366 (2007) 563-573
    • (2007) J. Mol. Biol. , vol.366 , pp. 563-573
    • Baek, K.1    Brown, R.S.2    Birrane, G.3    Ladias, J.A.4
  • 34
    • 1242342005 scopus 로고    scopus 로고
    • Evidence for conformational flexibility in the Tat-TAR recognition motif of cyclin T1
    • Das C., Edgcomb S.P., Peteranderl R., Chen L., and Frankel A.D. Evidence for conformational flexibility in the Tat-TAR recognition motif of cyclin T1. Virology 318 (2004) 306-317
    • (2004) Virology , vol.318 , pp. 306-317
    • Das, C.1    Edgcomb, S.P.2    Peteranderl, R.3    Chen, L.4    Frankel, A.D.5
  • 35
    • 0037062495 scopus 로고    scopus 로고
    • TAR RNA loop: a scaffold for the assembly of a regulatory switch in HIV replication
    • Richter S., Ping Y.H., and Rana T.M. TAR RNA loop: a scaffold for the assembly of a regulatory switch in HIV replication. Proc. Natl Acad. Sci. USA 99 (2005) 7928-7933
    • (2005) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7928-7933
    • Richter, S.1    Ping, Y.H.2    Rana, T.M.3
  • 36
    • 0032401752 scopus 로고    scopus 로고
    • Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat
    • Bieniasz P.D., Grdina T.A., Bogerd H.P., and Cullen B.R. Recruitment of a protein complex containing Tat and cyclin T1 to TAR governs the species specificity of HIV-1 Tat. EMBO J. 17 (1998) 7056-7065
    • (1998) EMBO J. , vol.17 , pp. 7056-7065
    • Bieniasz, P.D.1    Grdina, T.A.2    Bogerd, H.P.3    Cullen, B.R.4
  • 37
    • 0033574077 scopus 로고    scopus 로고
    • Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T
    • Fujinaga K., Taube R., Wimmer J., Cujec T.P., and Peterlin B.M. Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T. Proc. Natl Acad. Sci. USA 96 (1999) 1285-1290
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1285-1290
    • Fujinaga, K.1    Taube, R.2    Wimmer, J.3    Cujec, T.P.4    Peterlin, B.M.5
  • 38
    • 0346095303 scopus 로고    scopus 로고
    • Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element
    • Fujinaga K., Irwin D., Huang Y., Taube R., Kurosu T., and Peterlin B.M. Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element. Mol. Cell. Biol. 24 (2004) 787-795
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 787-795
    • Fujinaga, K.1    Irwin, D.2    Huang, Y.3    Taube, R.4    Kurosu, T.5    Peterlin, B.M.6
  • 39
    • 33646835410 scopus 로고    scopus 로고
    • HIV-1 Tat is a natively unfolded protein: the solution conformation and dynamics of reduced HIV-1 Tat (1-72) by NMR spectroscopy
    • Shojania S., and O'Neil J.D. HIV-1 Tat is a natively unfolded protein: the solution conformation and dynamics of reduced HIV-1 Tat (1-72) by NMR spectroscopy. J. Biol. Chem. 281 (2006) 8347-8356
    • (2006) J. Biol. Chem. , vol.281 , pp. 8347-8356
    • Shojania, S.1    O'Neil, J.D.2
  • 40
    • 0036133174 scopus 로고    scopus 로고
    • Interaction between P-TEFb and the C-terminal domain of RNA polymerase II activates transcriptional elongation from sites upstream or downstream of target genes
    • Taube R., Lin X., Irwin D., Fujinaga K., and Peterlin B. M. Interaction between P-TEFb and the C-terminal domain of RNA polymerase II activates transcriptional elongation from sites upstream or downstream of target genes. Mol. Cell. Biol. 22 (2002) 321-331
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 321-331
    • Taube, R.1    Lin, X.2    Irwin, D.3    Fujinaga, K.4    Peterlin, B. M.5
  • 41
    • 21644468867 scopus 로고    scopus 로고
    • Identification of a cyclin T-binding domain in Hexim1 and biochemical analysis of its binding competition with HIV-1 Tat
    • Schulte A., Czudnochowski N., Barboric M., Schonichen A., Blazek D., Peterlin B.M., and Geyer M. Identification of a cyclin T-binding domain in Hexim1 and biochemical analysis of its binding competition with HIV-1 Tat. J. Biol. Chem. 280 (2005) 24968-24977
    • (2005) J. Biol. Chem. , vol.280 , pp. 24968-24977
    • Schulte, A.1    Czudnochowski, N.2    Barboric, M.3    Schonichen, A.4    Blazek, D.5    Peterlin, B.M.6    Geyer, M.7
  • 42
    • 23344437022 scopus 로고    scopus 로고
    • Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
    • Li Q., Price J.P., Byers S.A., Cheng D., Peng J., and Price D.H. Analysis of the large inactive P-TEFb complex indicates that it contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFb molecules containing Cdk9 phosphorylated at threonine 186. J. Biol. Chem. 280 (2005) 28819-28826
    • (2005) J. Biol. Chem. , vol.280 , pp. 28819-28826
    • Li, Q.1    Price, J.P.2    Byers, S.A.3    Cheng, D.4    Peng, J.5    Price, D.H.6
  • 43
    • 34247874793 scopus 로고    scopus 로고
    • Tat competes with HEXIM1 to increase the active pool of P-TEFb for HIV-1 transcription
    • Barboric M., Yik J.H., Czudnochowski N., Yang Z., Chen R., Contreras X., et al. Tat competes with HEXIM1 to increase the active pool of P-TEFb for HIV-1 transcription. Nucl. Acids Res. 35 (2007) 2003-2012
    • (2007) Nucl. Acids Res. , vol.35 , pp. 2003-2012
    • Barboric, M.1    Yik, J.H.2    Czudnochowski, N.3    Yang, Z.4    Chen, R.5    Contreras, X.6
  • 44
    • 30644478471 scopus 로고    scopus 로고
    • Regulation of polymerase II transcription by 7SK snRNA: two distinct RNA elements direct P-TEFb and HEXIM1 binding
    • Egloff S., Van Herreweghe E., and Kiss T. Regulation of polymerase II transcription by 7SK snRNA: two distinct RNA elements direct P-TEFb and HEXIM1 binding. Mol. Cell. Biol. 26 (2006) 630-642
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 630-642
    • Egloff, S.1    Van Herreweghe, E.2    Kiss, T.3
  • 45
    • 10744222241 scopus 로고    scopus 로고
    • Structure-based drug design targeting an inactive RNA conformation: exploiting the flexibility of HIV-1 TAR RNA
    • Murchie A.I., Davis B., Isel C., Afshar M., Drysdale M.J., Bower J., et al. Structure-based drug design targeting an inactive RNA conformation: exploiting the flexibility of HIV-1 TAR RNA. J. Mol. Biol. 336 (2004) 625-638
    • (2004) J. Mol. Biol. , vol.336 , pp. 625-638
    • Murchie, A.I.1    Davis, B.2    Isel, C.3    Afshar, M.4    Drysdale, M.J.5    Bower, J.6
  • 46
    • 33646185063 scopus 로고    scopus 로고
    • Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1
    • Schonichen A., Alexander M., Gasteier J.E., Cuesta F.E., Fackler O.T., and Geyer M. Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. J. Biol. Chem. 281 (2006) 5084-5093
    • (2006) J. Biol. Chem. , vol.281 , pp. 5084-5093
    • Schonichen, A.1    Alexander, M.2    Gasteier, J.E.3    Cuesta, F.E.4    Fackler, O.T.5    Geyer, M.6
  • 47
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26 (1993) 795-800
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 48
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • Yeates T.O. Detecting and overcoming crystal twinning. Methods Enzymol. 276 (1997) 344-358
    • (1997) Methods Enzymol. , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 49
    • 0028103275 scopus 로고
    • CCP4 Collaborative Computational Project number 4
    • CCP4 Collaborative Computational Project number 4. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 51
  • 52
    • 13244281317 scopus 로고    scopus 로고
    • COOT: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. COOT: model-building tools for molecular graphics. Acta Crystallog. sect. D. 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 53
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 54
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • Diederichs K., and Karplus P.A. Improved R-factors for diffraction data analysis in macromolecular crystallography. Nature Struct. Biol. 4 (1997) 269-275
    • (1997) Nature Struct. Biol. , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2


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