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Volumn 72, Issue 6, 1998, Pages 4841-4848

Structure-based mutational analysis of the C-terminal DNA-binding domain of human immunodeficiency virus type 1 integrase: Critical residues for protein oligomerization and DNA binding

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRASE; VIRUS ENZYME;

EID: 0001166515     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.6.4841-4848.1998     Document Type: Article
Times cited : (122)

References (73)
  • 1
    • 0028863151 scopus 로고
    • Multimerization determinants reside in both the catalytic core and C terminus of avian sarcoma virus integrase
    • Andrake, M. D., and A. M. Skalka. 1995. Multimerization determinants reside in both the catalytic core and C terminus of avian sarcoma virus integrase. J. Biol. Chem. 270:29299-29306.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29299-29306
    • Andrake, M.D.1    Skalka, A.M.2
  • 2
    • 0029814410 scopus 로고    scopus 로고
    • Retroviral integrases, putting the pieces together
    • Andrake, M. D., and A. M. Skalka. 1996. Retroviral integrases, putting the pieces together. J. Biol. Chem. 271:19633-19636.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19633-19636
    • Andrake, M.D.1    Skalka, A.M.2
  • 3
    • 0028911769 scopus 로고
    • DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus
    • Baumann, H., S. Knapp, A. Karshikoff, R. Ladenstein, and T. Hard. 1995. DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus. J. Mol. Biol. 247:840-846.
    • (1995) J. Mol. Biol. , vol.247 , pp. 840-846
    • Baumann, H.1    Knapp, S.2    Karshikoff, A.3    Ladenstein, R.4    Hard, T.5
  • 4
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
    • Baumann, H., S. Knapp, T. Lundback, R. Ladenstein, and T. Hard. 1994. Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Nat. Struct. Biol. 1:808-819.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 808-819
    • Baumann, H.1    Knapp, S.2    Lundback, T.3    Ladenstein, R.4    Hard, T.5
  • 5
    • 0030566832 scopus 로고    scopus 로고
    • The catalytic domain of human immunodeficiency virus integrase: Ordered active site in the F185H mutant
    • Bujacz, G., J. Alexandratos, Q. Zhou-Liu, C. Clement-Mella, and A. Wlodawer. 1996. The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant. FEBS Lett. 398:175-178.
    • (1996) FEBS Lett. , vol.398 , pp. 175-178
    • Bujacz, G.1    Alexandratos, J.2    Zhou-Liu, Q.3    Clement-Mella, C.4    Wlodawer, A.5
  • 7
    • 0029643858 scopus 로고    scopus 로고
    • The catalytic domain of avian sarcoma virus integrase: Conformation of the active-site residues in the presence of divalent cations
    • Bujacz, G., M. Jaskolski, J. Alexandratos, A. Wlodawer, G. Merkel, R. A. Katz, and A. M. Skalka. 1996. The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. Structure 4:89-96.
    • (1996) Structure , vol.4 , pp. 89-96
    • Bujacz, G.1    Jaskolski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5    Katz, R.A.6    Skalka, A.M.7
  • 9
    • 0026568640 scopus 로고
    • Integration of human immunodeficiency virus DNA: Adduct interference analysis of required DNA sites
    • Bushman, F. D., and R. Craigie. 1992. Integration of human immunodeficiency virus DNA: adduct interference analysis of required DNA sites. Proc. Natl. Acad. Sci. USA 89:3458-3462.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3458-3462
    • Bushman, F.D.1    Craigie, R.2
  • 10
    • 0027456715 scopus 로고
    • Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding
    • Bushman, F. D., A. Engelman, I. Palmer, P. Wingfield, and R. Craigie. 1993. Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding. Proc. Natl. Acad. Sci. USA 90:3428-3432.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Palmer, I.3    Wingfield, P.4    Craigie, R.5
  • 12
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus
    • Chow, S. A., K. A. Vincent, V. Ellison, and P. O. Brown. 1992. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science 255:723-726.
    • (1992) Science , vol.255 , pp. 723-726
    • Chow, S.A.1    Vincent, K.A.2    Ellison, V.3    Brown, P.O.4
  • 13
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G. B., R. Ren, and D. Baltimore. 1995. Modular binding domains in signal transduction proteins. Cell 80:237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 15
    • 0026740842 scopus 로고
    • Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 in protein in vitro
    • Drelich, M., R. Wilhelm, and J. Mous. 1992. Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 IN protein in vitro. Virology 188:459-468.
    • (1992) Virology , vol.188 , pp. 459-468
    • Drelich, M.1    Wilhelm, R.2    Mous, J.3
  • 16
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda, F., A. B. Hickman, T. M. Jenkins, A. Engelman, R. Craigie, and D. R. Davies. 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
  • 17
    • 0028839434 scopus 로고
    • Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acido-caldarius
    • Edmondson, S. P., L. Qiu, and J. W. Shriver. 1995. Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acido-caldarius. Biochemistry 34:13289-13304.
    • (1995) Biochemistry , vol.34 , pp. 13289-13304
    • Edmondson, S.P.1    Qiu, L.2    Shriver, J.W.3
  • 20
    • 0028239062 scopus 로고
    • A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro
    • Ellison, V., and P. O. Brown. 1994. A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro. Proc. Natl. Acad. Sci. USA 91:7316-7320.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7316-7320
    • Ellison, V.1    Brown, P.O.2
  • 21
    • 0027179694 scopus 로고
    • Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex
    • Engelman, A., F. D. Bushman, and R. Craigie. 1993. Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex. EMBO J. 12:3269-3275.
    • (1993) EMBO J. , vol.12 , pp. 3269-3275
    • Engelman, A.1    Bushman, F.D.2    Craigie, R.3
  • 22
    • 0026649557 scopus 로고
    • Identification of amino acid residues critical for human immunodeficiency virus type 1 protein in vitro
    • Engelman, A., and R. Craigie. 1992. Identification of amino acid residues critical for human immunodeficiency virus type 1 protein in vitro. J. Virol. 66: 6361-6369.
    • (1992) J. Virol. , vol.66 , pp. 6361-6369
    • Engelman, A.1    Craigie, R.2
  • 23
    • 0028067324 scopus 로고
    • The core and carboxyl-terminal domains of the integrase protein of human immunodeficiency virus type 1 each contribute to nonspecific DNA binding
    • Engelman, A., A. B. Hickman, and R. Craigie. 1994. The core and carboxyl-terminal domains of the integrase protein of human immunodeficiency virus type 1 each contribute to nonspecific DNA binding. J. Virol. 68:5911-5917.
    • (1994) J. Virol. , vol.68 , pp. 5911-5917
    • Engelman, A.1    Hickman, A.B.2    Craigie, R.3
  • 24
    • 0025053617 scopus 로고
    • Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences?
    • Fayet, O., P. Ramond, P. Polard, M. F. Prere, and M. Chandler. 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
  • 25
    • 0027102597 scopus 로고
    • Genetics of retroviral integration
    • Goff, S. P. 1992. Genetics of retroviral integration. Annu. Rev. Genet. 26: 527-544.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 527-544
    • Goff, S.P.1
  • 26
    • 0029609126 scopus 로고
    • DNA transposition: From a black box to a color monitor
    • Grindley, N. D., and A. E. Leschziner. 1995. DNA transposition: from a black box to a color monitor. Cell 83:1063-1066.
    • (1995) Cell , vol.83 , pp. 1063-1066
    • Grindley, N.D.1    Leschziner, A.E.2
  • 27
    • 0027973067 scopus 로고
    • Biophysical and enzymatic properties of the catalytic domain of HIV-1 integrase
    • Hickman, A. B., I. Palmer, A. Engelman, R. Craigie, and P. Wingfield. 1994. Biophysical and enzymatic properties of the catalytic domain of HIV-1 integrase. J. Biol. Chem. 269:29279-29287.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29279-29287
    • Hickman, A.B.1    Palmer, I.2    Engelman, A.3    Craigie, R.4    Wingfield, P.5
  • 28
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higushi, R., B. Krummel, and R. K. Saiki. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16:7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higushi, R.1    Krummel, B.2    Saiki, R.K.3
  • 30
    • 0030828521 scopus 로고    scopus 로고
    • Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking
    • Jenkins, T. M., D. Esposito, A. Engelman, and R. Craigie. 1997. Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking. EMBO J. 16:6849-6859.
    • (1997) EMBO J. , vol.16 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 31
    • 0029017919 scopus 로고
    • Catalytic domain of human immunodeficiency virus type 1 integrase: Identification of a soluble mutant by systematic replacement of hydrophobic residues
    • Jenkins, T. M., A. Hickman, F. Dyda, R. Ghirlando, D. R. Davies, and R. Craigie. 1995. Catalytic domain of human immunodeficiency virus type 1 integrase: identification of a soluble mutant by systematic replacement of hydrophobic residues. Proc. Natl. Acad. Sci. USA 92:6057-6061.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6057-6061
    • Jenkins, T.M.1    Hickman, A.2    Dyda, F.3    Ghirlando, R.4    Davies, D.R.5    Craigie, R.6
  • 32
    • 2642604727 scopus 로고
    • Computer analysis of retroviral pol genes: Assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes
    • Johnson, M. S., M. A. McClure, D.-F. Feng, J. Gray, and R. F. Doolittle. 1986. Computer analysis of retroviral pol genes: assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes. Proc. Natl. Acad. Sci. USA 83:7548-7652.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7548-7652
    • Johnson, M.S.1    McClure, M.A.2    Feng, D.-F.3    Gray, J.4    Doolittle, R.F.5
  • 33
    • 0026665238 scopus 로고
    • Retroviral integrase functions as a multimer and can turn over catalytically
    • Jones, K. S., J. Coleman, G. W. Merkel, T. M. Laue, and A. M. Skalka. 1994. Retroviral integrase functions as a multimer and can turn over catalytically. J. Biol. Chem. 287:16037-16040.
    • (1994) J. Biol. Chem. , vol.287 , pp. 16037-16040
    • Jones, K.S.1    Coleman, J.2    Merkel, G.W.3    Laue, T.M.4    Skalka, A.M.5
  • 34
    • 0027525261 scopus 로고
    • Genetic analysis of homomeric interactions of human immunodeficiency virus type 1 integrase using the yeast two-hybrid system
    • Kalpana, G. V., and S. Goff. 1993. Genetic analysis of homomeric interactions of human immunodeficiency virus type 1 integrase using the yeast two-hybrid system. Proc. Natl. Acad. Sci. USA 90:10593-10597.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10593-10597
    • Kalpana, G.V.1    Goff, S.2
  • 35
    • 0028566214 scopus 로고
    • Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5
    • Kalpana, G. V., S. Marmon, W. Wang, G. R. Crabtree, and S. P. Goff. 1994. Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5. Science 266:2002-2006.
    • (1994) Science , vol.266 , pp. 2002-2006
    • Kalpana, G.V.1    Marmon, S.2    Wang, W.3    Crabtree, G.R.4    Goff, S.P.5
  • 37
    • 0026035178 scopus 로고
    • Retroviral integrase domains: DNA binding and the recognition of LTR sequences
    • Khan, E., J. P. G. Mack, R. A. Katz, J. Kulkosky, and A. M. Skalka. 1991. Retroviral integrase domains: DNA binding and the recognition of LTR sequences. Nucleic Acids Res. 19:851-860.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 851-860
    • Khan, E.1    Mack, J.P.G.2    Katz, R.A.3    Kulkosky, J.4    Skalka, A.M.5
  • 38
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 39
    • 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., K. S. Jones, R. A. Katz, J. P. G. Mack, and A. M. Skalka. 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
  • 40
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan, J., and D. Cowburn. 1997. Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26:259-288.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 41
    • 0026072804 scopus 로고
    • Substrate specificity of recombinant human immunodeficiency virus integrase protein
    • LaFemina, R. L., P. L. Callahan, and M. G. Cordingley. 1991. Substrate specificity of recombinant human immunodeficiency virus integrase protein. J. Virol. 65:5624-5630.
    • (1991) J. Virol. , vol.65 , pp. 5624-5630
    • LaFemina, R.L.1    Callahan, P.L.2    Cordingley, M.G.3
  • 42
    • 0030458494 scopus 로고    scopus 로고
    • An atomic view of the L-tryptophan binding site of trp repressor
    • Lawson, C. L. 1996. An atomic view of the L-tryptophan binding site of trp repressor. Nat. Struct. Biol. 3:986-987.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 986-987
    • Lawson, C.L.1
  • 43
    • 0030614408 scopus 로고    scopus 로고
    • Zn promotes the self-association of human immunodeficiency virus integrase in vitro
    • Lee, S. P., J. Xiao, J. R. Knutson, M. S. Lewis, and M. K. Han. 1997. Zn promotes the self-association of human immunodeficiency virus integrase in vitro. Biochemistry 36:173-180.
    • (1997) Biochemistry , vol.36 , pp. 173-180
    • Lee, S.P.1    Xiao, J.2    Knutson, J.R.3    Lewis, M.S.4    Han, M.K.5
  • 45
    • 0029281993 scopus 로고
    • SH3 domains. Minding your p's and q's
    • Mayer, B. J., and M. J. Eck. 1995. SH3 domains. Minding your p's and q's. Curr. Biol. 5:364-367.
    • (1995) Curr. Biol. , vol.5 , pp. 364-367
    • Mayer, B.J.1    Eck, M.J.2
  • 46
    • 0028352363 scopus 로고
    • Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase
    • Mazumder, A., A. Engelman, R. Craigie, M. Fesen, and Y. Pommier. 1994. Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase. Nucleic Acids Res. 22:1037-1043.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1037-1043
    • Mazumder, A.1    Engelman, A.2    Craigie, R.3    Fesen, M.4    Pommier, Y.5
  • 47
    • 0030628279 scopus 로고    scopus 로고
    • Polynucleotidyl transfer reactions in site-specific DNA recombination
    • Mizuuchi, K. 1997. Polynucleotidyl transfer reactions in site-specific DNA recombination. Genes Cells 2:1-12.
    • (1997) Genes Cells , vol.2 , pp. 1-12
    • Mizuuchi, K.1
  • 48
    • 0026081040 scopus 로고
    • Defining nucleic acid-binding properties of avian retrovirus integrase by deletion analysis
    • Mumm, S. R., and D. P. Grandgenett. 1991. Defining nucleic acid-binding properties of avian retrovirus integrase by deletion analysis. J. Virol. 65: 1160-1167.
    • (1991) J. Virol. , vol.65 , pp. 1160-1167
    • Mumm, S.R.1    Grandgenett, D.P.2
  • 49
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio, A., M. Saraste, and M. Wilmanns. 1994. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat. Struct. Biol. 1:546-551.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 51
    • 0028034050 scopus 로고
    • Characterization of the minimal DNA-binding domain of the HIV integrase protein
    • Puras Lutzke, R. A., C. Vink, and R. H. A. Plasterk. 1994. Characterization of the minimal DNA-binding domain of the HIV integrase protein. Nucleic Acids Res. 22:4125-4131.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4125-4131
    • Puras Lutzke, R.A.1    Vink, C.2    Plasterk, R.H.A.3
  • 53
    • 0026634793 scopus 로고
    • The N-terminal region of HIV-1 integrase is required for integration activity, but not for DNA-binding
    • Schauer, M., and A. Billich. 1992. The N-terminal region of HIV-1 integrase is required for integration activity, but not for DNA-binding. Biochem. Biophys. Res. Commun. 186:874-888.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 874-888
    • Schauer, M.1    Billich, A.2
  • 54
    • 0031050297 scopus 로고    scopus 로고
    • Disruption of the terminal base pairs of retroviral DNA during integration
    • Scottoline, B. P., S. A. Chow, V. Ellison, and P. O. Brown. 1997. Disruption of the terminal base pairs of retroviral DNA during integration. Genes Dev. 11:371-382.
    • (1997) Genes Dev. , vol.11 , pp. 371-382
    • Scottoline, B.P.1    Chow, S.A.2    Ellison, V.3    Brown, P.O.4
  • 55
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., I. Moarefi, and J. Kuriyan. 1997. Crystal structure of the Src family tyrosine kinase Hck. Nature 385:602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 56
    • 0028089732 scopus 로고
    • DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein
    • van den Ent, F. M., C. Vink, and R. H. Plasterk. 1994. DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein. J. Virol. 68:7825-7832.
    • (1994) J. Virol. , vol.68 , pp. 7825-7832
    • Van Den Ent, F.M.1    Vink, C.2    Plasterk, R.H.3
  • 57
    • 0031965842 scopus 로고    scopus 로고
    • Mutational scan of the human immunodeficiency virus type 2 integrase protein
    • van den Ent, F. M. I., A. Vos, and R. H. A. Plasterk. 1998. Mutational scan of the human immunodeficiency virus type 2 integrase protein. J. Virol. 72:3916-3924.
    • (1998) J. Virol. , vol.72 , pp. 3916-3924
    • Van Den Ent, F.M.I.1    Vos, A.2    Plasterk, R.H.A.3
  • 58
    • 0025775488 scopus 로고
    • DNA binding properties of the integrase proteins of human immunodeficiency viruses type 1 and 2
    • van Gent, D. C., Y. Elgersma, M. W. J. Bolk, C. Vink, and R. H. A. Plasterk. 1991. DNA binding properties of the integrase proteins of human immunodeficiency viruses type 1 and 2. Nucleic Acids Res. 19:3821-3827.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3821-3827
    • Van Gent, D.C.1    Elgersma, Y.2    Bolk, M.W.J.3    Vink, C.4    Plasterk, R.H.A.5
  • 59
    • 0027179416 scopus 로고
    • Identification of amino acids in HIV-2 integrase involved in site-specific hydrolysis and alcoholysis of viral DNA termini
    • van Gent, D. C., A. A. Oude Groeneger, and R. H. Plasterk. 1993 Identification of amino acids in HIV-2 integrase involved in site-specific hydrolysis and alcoholysis of viral DNA termini. Nucleic Acids Res. 21:3373-3377.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3373-3377
    • Van Gent, D.C.1    Oude Groeneger, A.A.2    Plasterk, R.H.3
  • 60
    • 0027246609 scopus 로고
    • Complementation between HIV integrase proteins mutated in different domains
    • van Gent, D. C., C. Vink, A. A. M. Oude Groeneger, and R. H. A. Plasterk. 1993. Complementation between HIV integrase proteins mutated in different domains. EMBO J. 12:3261-3267.
    • (1993) EMBO J. , vol.12 , pp. 3261-3267
    • Van Gent, D.C.1    Vink, C.2    Oude Groeneger, A.A.M.3    Plasterk, R.H.A.4
  • 61
    • 0030779907 scopus 로고    scopus 로고
    • Crystal structure of the specific DNA binding domain of Tc3 transposase of C. elegans in complex with transposon DNA
    • in press
    • van Pouderoyen, G., R. F. Ketting, A. Perrakis, R. H. A. Plasterk, and T. K. Sixma. Crystal structure of the specific DNA binding domain of Tc3 transposase of C. elegans in complex with transposon DNA. EMBO J., in press.
    • EMBO J.
    • Van Pouderoyen, G.1    Ketting, R.F.2    Perrakis, A.3    Plasterk, R.H.A.4    Sixma, T.K.5
  • 62
    • 0027210608 scopus 로고
    • Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type 1 integrase protein
    • Vink, C., A. A. M. Oude Groeneger, and R. H. A. Plasterk. 1993. Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type 1 integrase protein. Nucleic Acids Res. 21:1419-1425.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude Groeneger, A.A.M.2    Plasterk, R.H.A.3
  • 63
    • 0027508068 scopus 로고
    • The human immunodeficiency virus integrase protein
    • Vink, C., and R. H. A. Plasterk. 1993. The human immunodeficiency virus integrase protein. Trends Genet. 9:433-437.
    • (1993) Trends Genet. , vol.9 , pp. 433-437
    • Vink, C.1    Plasterk, R.H.A.2
  • 64
    • 0028125329 scopus 로고
    • Formation of a stable complex between the human immunodeficiency virus integrase protein and viral DNA
    • Vink, C., R. A. Puras Lutzke, and R. H. A. Plasterk. 1994. Formation of a stable complex between the human immunodeficiency virus integrase protein and viral DNA. Nucleic Acids Res. 22:4103-4110.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4103-4110
    • Vink, C.1    Puras Lutzke, R.A.2    Plasterk, R.H.A.3
  • 65
    • 0026095906 scopus 로고
    • Human immunodeficiency virus integrase protein requires a subterminal position of its viral DNA recognition sequence for efficient cleavage
    • Vink, C., D. C. van Gent, Y. Elgersma, and R. H. A. Plasterk. 1991. Human immunodeficiency virus integrase protein requires a subterminal position of its viral DNA recognition sequence for efficient cleavage. J. Virol. 65:4636-4644.
    • (1991) J. Virol. , vol.65 , pp. 4636-4644
    • Vink, C.1    Van Gent, D.C.2    Elgersma, Y.3    Plasterk, R.H.A.4
  • 66
    • 0026622006 scopus 로고
    • Retroviral reverse transcription and integration: Progress and problems
    • Whitcomb, J. M., and S. H. Hughes. 1992. Retroviral reverse transcription and integration: progress and problems. Annu. Rev. Cell Biol. 8:275-306.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 275-306
    • Whitcomb, J.M.1    Hughes, S.H.2
  • 67
    • 0026539155 scopus 로고
    • Localization of DNA binding activity of HIV-1 integrase to the C-terminal half of the protein
    • Woerner, A. M., M. Klutch, J. G. Levin, and C. J. Marcus-Secura. 1992. Localization of DNA binding activity of HIV-1 integrase to the C-terminal half of the protein. AIDS Res. Hum. Retroviruses 8:297-304.
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , pp. 297-304
    • Woerner, A.M.1    Klutch, M.2    Levin, J.G.3    Marcus-Secura, C.J.4
  • 68
    • 0027205243 scopus 로고
    • Characterization of a DNA binding domain in the C-terminus of HIV-1 integrase by deletion mutagenesis
    • Woerner, A. M., and C. J. Marcus-Secura. 1993. Characterization of a DNA binding domain in the C-terminus of HIV-1 integrase by deletion mutagenesis. Nucleic Acids Res. 21:3507-3511.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3507-3511
    • Woerner, A.M.1    Marcus-Secura, C.J.2
  • 69
    • 0029151254 scopus 로고
    • A novel DNA binding and nuclease activity in domain III of Mu transposase: Evidence for a catalytic region involved in donor cleavage
    • Wu, Z., and G. Chaconas. 1995. A novel DNA binding and nuclease activity in domain III of Mu transposase: evidence for a catalytic region involved in donor cleavage. EMBO J. 14:3835-3843.
    • (1995) EMBO J. , vol.14 , pp. 3835-3843
    • Wu, Z.1    Chaconas, G.2
  • 70
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., S. C. Harrison, and M. J. Eck. 1997. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385:595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 71
    • 0028919759 scopus 로고
    • Crystal structure of a paired domain-DNA complex at 2.5 a resolution reveals structural basis for Pax developmental mutations
    • Xu, W., M. A. Rould, S. Jun, C. Desplan, and C. O. Pabo. 1995. Crystal structure of a paired domain-DNA complex at 2.5 A 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
  • 72
    • 0029643952 scopus 로고
    • Recombining the structures of integrase, RuvC and RNaseH
    • Yang, W., and T. A. Steitz. 1995. Recombining the structures of integrase, RuvC and RNaseH. Structure 3:131-134.
    • (1995) Structure , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 73
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng, R., T. M. Jenkins, and R. Craigie. 1996. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc. Natl. Acad. Sci. USA 93:13659-13664.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3


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