메뉴 건너뛰기




Volumn 16, Issue 19, 1997, Pages 6044-6054

Crystal structure of the specific DNA-binding domain of Tc3 transposase of C.elegans in complex with transposon DNA

Author keywords

Crystal structure; DNA binding; Helix turn helix; Tc1; Tc3 transposase

Indexed keywords

DIMER; HELIX LOOP HELIX PROTEIN; HELMINTH DNA; TRANSPOSASE;

EID: 0030779907     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.19.6044     Document Type: Article
Times cited : (91)

References (70)
  • 1
    • 0029871975 scopus 로고    scopus 로고
    • The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis
    • Aldaz,H., Schuster,E. and Baker,T.A. (1996) The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis. Cell, 85, 257-269.
    • (1996) Cell , vol.85 , pp. 257-269
    • Aldaz, H.1    Schuster, E.2    Baker, T.A.3
  • 2
    • 0028120546 scopus 로고
    • Atomic structure of the RuvC resolvase: A Holliday junction-specific endonuclease from E.coli
    • Ariyoshi,M., Vassylyev,D.G., Iwasaki,H., Nakamura,H., Shinagawa,H. and Morikawa,K. (1994) Atomic structure of the RuvC resolvase: a Holliday junction-specific endonuclease from E.coli. Cell, 78, 1063-1072.
    • (1994) Cell , vol.78 , pp. 1063-1072
    • Ariyoshi, M.1    Vassylyev, D.G.2    Iwasaki, H.3    Nakamura, H.4    Shinagawa, H.5    Morikawa, K.6
  • 3
    • 0028317055 scopus 로고
    • Identification of residues in the Mu transposase essential for catalysis
    • Baker,T.A. and Luo,L. (1994) Identification of residues in the Mu transposase essential for catalysis. Proc. Natl Acad. Sci. USA, 91, 6654-6658.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6654-6658
    • Baker, T.A.1    Luo, L.2
  • 5
    • 0026657433 scopus 로고
    • Refined 1.8 Å crystal structure of the λ, represser-operator complex
    • Beamer,L.J. and Pabo,C.O. (1992) Refined 1.8 Å crystal structure of the λ, represser-operator complex. J. Mol. Biol., 227, 177-196.
    • (1992) J. Mol. Biol. , vol.227 , pp. 177-196
    • Beamer, L.J.1    Pabo, C.O.2
  • 7
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger,A.T. (1992b) 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
  • 9
    • 0030199188 scopus 로고    scopus 로고
    • DNA transposition: Jumping gene machine, some assembly required
    • Chaconas,G., Lavoie,B.D. and Watson,M.A. (1996) DNA transposition: jumping gene machine, some assembly required. Curr. Biol., 6, 817-820.
    • (1996) Curr. Biol. , vol.6 , pp. 817-820
    • Chaconas, G.1    Lavoie, B.D.2    Watson, M.A.3
  • 10
    • 0028608962 scopus 로고
    • DNA binding activities of the Caenorhabditis elegans Tc3 transposase
    • Colloms,S.D., van Luenen,H.G.A.M. and Plasterk,R.H.A. (1994) DNA binding activities of the Caenorhabditis elegans Tc3 transposase. Nucleic Acids Res., 22, 5548-5554.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5548-5554
    • Colloms, S.D.1    Van Luenen, H.G.A.M.2    Plasterk, R.H.A.3
  • 11
    • 0027426925 scopus 로고
    • DNA sequence recognition by Pax proteins: Bipartite structure of the paired domain and its binding site
    • Czerny,T., Schaffner,G. and Busslinger,M. (1993) DNA sequence recognition by Pax proteins: bipartite structure of the paired domain and its binding site. Genes Dev., 7, 2048-2061.
    • (1993) Genes Dev. , vol.7 , pp. 2048-2061
    • Czerny, T.1    Schaffner, G.2    Busslinger, M.3
  • 12
    • 0028053230 scopus 로고
    • A proposed superfamily of transposase genes: Transposon-like elements in ciliated protozoa and a common 'D35E' motif
    • Doak,T.G., Doerder,F.P., Jahn,C.L. and Herrick,G. (1994) A proposed superfamily of transposase genes: transposon-like elements in ciliated protozoa and a common 'D35E' motif. Proc. Natl Acad. Sci. USA, 91, 942-946.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 942-946
    • Doak, T.G.1    Doerder, F.P.2    Jahn, C.L.3    Herrick, G.4
  • 14
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda,F., Hickman,A.B., Jenkins,T.M., Engelman,A., Craigie,R. and Davies,D.R. (1994) Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science, 266, 1981-1986.
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 15
    • 0031260521 scopus 로고    scopus 로고
    • The solution structure of the N-terminal HHCC domain of HIV-2 integrase: A three-helix bundle stabilized by zinc
    • in press
    • Eijkelenboom,A.P.A.M. (1997) The solution structure of the N-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc. Curr. Biol., in press.
    • (1997) Curr. Biol.
    • Eijkelenboom, A.P.A.M.1
  • 16
    • 0028239775 scopus 로고
    • Identification of a Pax paired domain recognition sequence and evidence for DNA-dependent conformational changes
    • Epstein,J., Cai,J., Glaser,T., Jepeal,L. and Maas,R. (1994a) Identification of a Pax paired domain recognition sequence and evidence for DNA-dependent conformational changes. J. Biol. Chem., 269, 8355-8361.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8355-8361
    • Epstein, J.1    Cai, J.2    Glaser, T.3    Jepeal, L.4    Maas, R.5
  • 17
    • 0028096639 scopus 로고
    • Two independent and interactive DNA-binding subdomains of the Pax6 paired domain are regulated by alternative splicing
    • Epstein,J.A., Glaser,T., Cai,J., Jepeal,L., Walton,D.S. and Maas,R.L. (1994b) Two independent and interactive DNA-binding subdomains of the Pax6 paired domain are regulated by alternative splicing. Genes Dev., 8, 2022-2034.
    • (1994) Genes Dev. , vol.8 , pp. 2022-2034
    • Epstein, J.A.1    Glaser, T.2    Cai, J.3    Jepeal, L.4    Walton, D.S.5    Maas, R.L.6
  • 18
    • 0025053617 scopus 로고
    • Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences?
    • Fayet,O., Ramond,P., Polard,P., Prere,M.F. and Chandler,M. (1990) Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences? Mol. Microbiol., 4, 1771-1777.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1771-1777
    • Fayet, O.1    Ramond, P.2    Polard, P.3    Prere, M.F.4    Chandler, M.5
  • 19
    • 0028118764 scopus 로고
    • Hin recombinase bound to DNA: The origin of specificity in major and minor groove interactions
    • Feng,J.-A., Johnson,R.C. and Dickerson,R.E. (1994) Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions. Science, 263, 348-355.
    • (1994) Science , vol.263 , pp. 348-355
    • Feng, J.-A.1    Johnson, R.C.2    Dickerson, R.E.3
  • 20
    • 0028226218 scopus 로고
    • Mobile Minos elements from Drosophila hydei encode a two-exon transposase with similarity to the paired DNA-binding domain
    • Franz,G., Loukeris,T.G., Dialektaki,G., Thompson,C.R.L. and Charalambos,S. (1994) Mobile Minos elements from Drosophila hydei encode a two-exon transposase with similarity to the paired DNA-binding domain. Proc. Natl Acad. Sci. USA, 91, 4746-4750.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4746-4750
    • Franz, G.1    Loukeris, T.G.2    Dialektaki, G.3    Thompson, C.R.L.4    Charalambos, S.5
  • 21
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French,S. and Wilson,K. (1978) On the treatment of negative intensity observations. Acta Crystallogr., A34, 517-525.
    • (1978) Acta Crystallogr. , vol.A34 , pp. 517-525
    • French, S.1    Wilson, K.2
  • 22
  • 23
    • 0017881332 scopus 로고
    • The α-helix dipole and the properties of proteins
    • Hol,W.G.J., van Duijnen,PT. and Berendsen,H.J.C. (1978) The α-helix dipole and the properties of proteins. Nature, 273, 443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 24
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm,L. and Sander,C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 25
    • 0029895619 scopus 로고    scopus 로고
    • Identification of functional domains and evolution of Tc/-like transposable elements
    • Ivies,I., Izsvak,Z., Minter,A. and Hackett,P.B. (1996) Identification of functional domains and evolution of Tc/-like transposable elements. Proc. Natl Acad. Sci. USA, 93, 5008-5013.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5008-5013
    • Ivies, I.1    Izsvak, Z.2    Minter, A.3    Hackett, P.B.4
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building 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 building models in electron density maps and the location of errors in these models. 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    Kjeldgaard, M.4
  • 30
    • 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
  • 31
    • 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
  • 32
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt,G.J. and Jones,T.A. (1996) Efficient rebuilding of protein structures. Acta Crystallogr., D52, 829-832.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 33
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis,P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 34
    • 0026719238 scopus 로고
    • Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases
    • Kulkosky,J., Jones,K.S., Katz,R.A., Mack,J.P.G. and Skalka,A.M. (1992) Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases. Mol. Cell. Biol., 12, 2331-2338.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2331-2338
    • Kulkosky, J.1    Jones, K.S.2    Katz, R.A.3    Mack, J.P.G.4    Skalka, A.M.5
  • 35
    • 0029818461 scopus 로고    scopus 로고
    • A purified mariner transposase is sufficient to mediate transposition in vitro
    • Lampe,D.J., Churchill,M.E.A. and Robertson,H.M. (1996) A purified mariner transposase is sufficient to mediate transposition in vitro. EMBO J., 15, 5470-5479.
    • (1996) EMBO J. , vol.15 , pp. 5470-5479
    • Lampe, D.J.1    Churchill, M.E.A.2    Robertson, H.M.3
  • 36
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin,V.S. and Wilson,K.S. (1993) Automated refinement of protein models. Acta Crystallogr., D49, 129-147.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 37
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • in press
    • Lamzin,V.S. and Wilson,K.S. (1997) Automated refinement for protein crystallography. Methods Enzymol., 277, in press.
    • (1997) Methods Enzymol. , vol.277
    • Lamzin, V.S.1    Wilson, K.S.2
  • 38
    • 0024539180 scopus 로고
    • Defining the structure of irregular nucleic acids: Conventions and principles
    • Lavery,R. and Sklenar,H. (1989) Defining the structure of irregular nucleic acids: conventions and principles. J. Biomol. Struct. Dyn., 6, 655-667.
    • (1989) J. Biomol. Struct. Dyn. , vol.6 , pp. 655-667
    • Lavery, R.1    Sklenar, H.2
  • 39
    • 0002359915 scopus 로고
    • DNA-protein interaction at high resolution
    • Lilley,D.M.J. (ed.). Oxford University Press, Oxford, UK
    • Luisi,B. (1995) DNA-protein interaction at high resolution. In Lilley,D.M.J. (ed.), DNA-Protein: Structural Interactions. Oxford University Press, Oxford, UK, pp. 1-48.
    • (1995) DNA-Protein: Structural Interactions , pp. 1-48
    • Luisi, B.1
  • 41
    • 0026652466 scopus 로고
    • A mutation at one end of Moloney murine leukemia virus DNA blocks cleavage of both ends by the viral integrase in vivo
    • Murphy,J.E. and Goff,S.P. (1992) A mutation at one end of Moloney murine leukemia virus DNA blocks cleavage of both ends by the viral integrase in vivo. J. Virol., 66, 5092-5095.
    • (1992) J. Virol. , vol.66 , pp. 5092-5095
    • Murphy, J.E.1    Goff, S.P.2
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov,G.N., Vagin,A.A. and Dodson,E.S. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr., D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.S.3
  • 43
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls,A., Sharp,K.A. and Honig,B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 44
    • 0028964702 scopus 로고
    • Comparison of the free and DNA-complexed forms of the DNA-binding domain from c-Myb
    • Ogata,K. et al. (1995) Comparison of the free and DNA-complexed forms of the DNA-binding domain from c-Myb. Struct. Biol., 2, 309-320.
    • (1995) Struct. Biol. , vol.2 , pp. 309-320
    • Ogata, K.1
  • 45
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer,L., Isaacs,N. and Bailey,S. (eds). SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski,Z. (1993) Oscillation data reduction program. In Sawyer,L., Isaacs,N. and Bailey,S. (eds), Proceedings of the CCP4 Study Weekend. Data Collection and Processing. SERC Daresbury Laboratory, Warrington, UK, pp. 56-62.
    • (1993) Proceedings of the CCP4 Study Weekend. Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 46
    • 0007284205 scopus 로고
    • Mechanisms of DNA transposition
    • Sherratt,D.J. (ed.). Oxford University Press, Oxford, UK
    • Plasterk,R.H.A. (1995) Mechanisms of DNA transposition. In Sherratt,D.J. (ed.), Mobile Genetic Elements. Oxford University Press, Oxford, UK, pp. 18-37.
    • (1995) Mobile Genetic Elements , pp. 18-37
    • Plasterk, R.H.A.1
  • 48
    • 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
  • 49
    • 0029129435 scopus 로고
    • Structure of the bacteriophage Mu transposase core: A common structural motif for DNA transposition and retroviral integration
    • Rice,P. and Mizuuchi,K. (1995) Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell, 82, 209-220.
    • (1995) Cell , vol.82 , pp. 209-220
    • Rice, P.1    Mizuuchi, K.2
  • 50
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost,B. and Sander,C. (1993) Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol., 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 51
    • 0029986753 scopus 로고    scopus 로고
    • Mu transpositional recombination: Donor DNA cleavage and strand transfer in trans by the Mu transposase
    • Savilahti,H. and Mizuuchi,K. (1996) Mu transpositional recombination: donor DNA cleavage and strand transfer in trans by the Mu transposase. Cell, 85, 271-280.
    • (1996) Cell , vol.85 , pp. 271-280
    • Savilahti, H.1    Mizuuchi, K.2
  • 52
    • 0028184697 scopus 로고
    • Measuring the geometry of DNA grooves
    • Stofer,E. and Lavery,R. (1994) Measuring the geometry of DNA grooves. Biopolymers, 34, 337-346.
    • (1994) Biopolymers , vol.34 , pp. 337-346
    • Stofer, E.1    Lavery, R.2
  • 53
    • 0028597967 scopus 로고
    • DNA bending by asymmetric phosphate neutralization
    • Strauss,J.K. and Maher,L.J. (1994) DNA bending by asymmetric phosphate neutralization. Science, 266, 1829-1834.
    • (1994) Science , vol.266 , pp. 1829-1834
    • Strauss, J.K.1    Maher, L.J.2
  • 54
    • 0027176645 scopus 로고
    • Common features in DNA recognition helices of eukaryotic transcription factors
    • Suzuki,M. (1993) Common features in DNA recognition helices of eukaryotic transcription factors. EMBO J., 12, 3221-3226.
    • (1993) EMBO J. , vol.12 , pp. 3221-3226
    • Suzuki, M.1
  • 55
    • 0029417120 scopus 로고
    • Binding geometry of α-helices that recognize DNA
    • Suzuki,M and Gerstein,M. (1995) Binding geometry of α-helices that recognize DNA. Proteins, 23, 525-535.
    • (1995) Proteins , vol.23 , pp. 525-535
    • Suzuki, M.1    Gerstein, M.2
  • 57
    • 0002518563 scopus 로고    scopus 로고
    • Knowledge-based B-factor restraints for the refinement of proteins
    • Tronrud,D.E. (1996) Knowledge-based B-factor restraints for the refinement of proteins. J. Appl. Crystallogr., 29, 100-104.
    • (1996) J. Appl. Crystallogr. , vol.29 , pp. 100-104
    • Tronrud, D.E.1
  • 58
    • 0029645904 scopus 로고
    • Homeodomains: Together again for the first time
    • Tullius,T. (1995) Homeodomains: together again for the first time. Structure, 15, 1143-1145.
    • (1995) Structure , vol.15 , pp. 1143-1145
    • Tullius, T.1
  • 59
    • 0027273429 scopus 로고
    • Mobilization of quiet, endogenous Tc3 transposons of Caenorhabditis elegans by forced expression of Tc3 transposase
    • van Luenen,H.G.A.M., Colloms,S.D. and Plasterk,R.H.A. (1993) Mobilization of quiet, endogenous Tc3 transposons of Caenorhabditis elegans by forced expression of Tc3 transposase. EMBO J., 12, 2513-2520.
    • (1993) EMBO J. , vol.12 , pp. 2513-2520
    • Van Luenen, H.G.A.M.1    Colloms, S.D.2    Plasterk, R.H.A.3
  • 60
    • 0028090258 scopus 로고
    • The mechanism of transposition of Tc3 of C.elegans
    • van Luenen,H.G.A.M., Colloms,S.D. and Plasterk,R.H.A. (1994) The mechanism of transposition of Tc3 of C.elegans. Cell, 79, 293-301.
    • (1994) Cell , vol.79 , pp. 293-301
    • Van Luenen, H.G.A.M.1    Colloms, S.D.2    Plasterk, R.H.A.3
  • 61
    • 0028598507 scopus 로고
    • Tel transposase of Caenorhabditis elegans is an endonuclease with a bipartite DNA-binding domain
    • Vos,J.C. and Plasterk,R.H.A. (1994) Tel transposase of Caenorhabditis elegans is an endonuclease with a bipartite DNA-binding domain. EMBO J., 13, 6125-6132.
    • (1994) EMBO J. , vol.13 , pp. 6125-6132
    • Vos, J.C.1    Plasterk, R.H.A.2
  • 62
    • 0027321357 scopus 로고
    • Characterization of the Caenorhabditis elegans Tc1 transposase in vivo and in vitro
    • Vos,J.C., van Luenen,H.G.A.M. and Plasterk,R.H.A. (1993) Characterization of the Caenorhabditis elegans Tc1 transposase in vivo and in vitro. Genes Dev., 7, 1244-1253.
    • (1993) Genes Dev. , vol.7 , pp. 1244-1253
    • Vos, J.C.1    Van Luenen, H.G.A.M.2    Plasterk, R.H.A.3
  • 63
    • 0029930255 scopus 로고    scopus 로고
    • Transposase is the only nematode protein required for in vitro transposition of Tel
    • Vos,J.C., De Baere,I. and Plasterk,R.H.A. (1996) Transposase is the only nematode protein required for in vitro transposition of Tel. Genes Dev., 10, 755-761.
    • (1996) Genes Dev. , vol.10 , pp. 755-761
    • Vos, J.C.1    De Baere, I.2    Plasterk, R.H.A.3
  • 64
    • 0001210234 scopus 로고
    • The probability distribution of X-ray intensities
    • Wilson,A.J.C. (1949) The probability distribution of X-ray intensities. Acta Crystallogr., 2, 318-321.
    • (1949) Acta Crystallogr. , vol.2 , pp. 318-321
    • Wilson, A.J.C.1
  • 65
    • 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
  • 66
    • 0030595337 scopus 로고    scopus 로고
    • Structural classification of HTH DNA-binding domains and protein-DNA interaction modes
    • Wintjens,R. and Rooman,M. (1996) Structural classification of HTH DNA-binding domains and protein-DNA interaction modes. J. Mol. Biol., 262, 294-313.
    • (1996) J. Mol. Biol. , vol.262 , pp. 294-313
    • Wintjens, R.1    Rooman, M.2
  • 67
    • 0028919759 scopus 로고
    • Crystal structure of a paired domain-DNA complex at 2.5 Å resolution reveals structural basis for Pax developmental mutations
    • Xu,W., Rould,M.A., Jun,S., Desplan,C. and Pabo,C.O. (1995) Crystal structure of a paired domain-DNA complex at 2.5 Å resolution reveals structural basis for Pax developmental mutations. Cell, 80, 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
  • 68
    • 0029943157 scopus 로고    scopus 로고
    • Positional information within the Mu transposase tetramer: Catalytic contributions of individual monomers
    • Yang,J.-Y., Jayaram,M. and Harshey,R.M. (1996) Positional information within the Mu transposase tetramer: catalytic contributions of individual monomers. Cell, 85, 447-455.
    • (1996) Cell , vol.85 , pp. 447-455
    • Yang, J.-Y.1    Jayaram, M.2    Harshey, R.M.3
  • 69
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • Yang,W. and Steitz,T. (1995) Recombining the structures of HIV integrase, RuvC and RNase H. Structure, 15, 131-134.
    • (1995) Structure , vol.15 , pp. 131-134
    • Yang, W.1    Steitz, T.2
  • 70
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein
    • Yang,W., Hendrickson,W.A., Crouch,R.J. and Satow,Y (1990) Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein. Science, 249, 1398-1405.
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.