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Volumn 4, Issue 7, 1997, Pages 567-577

Solution structure of the N-terminal zinc binding domain of HIV-1 integrase

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; DIMER; DNA BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; HISTIDINE; INTEGRASE; MONOMER; VIRUS ENZYME; ZINC;

EID: 0030986376     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0797-567     Document Type: Article
Times cited : (312)

References (65)
  • 1
    • 0026622006 scopus 로고
    • Retrovira! reverse transcription and integration: Progress and problems
    • Whitcomb, J.M. & Hughes, S.H. Retrovira! reverse transcription and integration: progress and problems. Anna. Rev. Cell Biol. 8, 275-306 (1992).
    • (1992) Anna. Rev. Cell Biol. , vol.8 , pp. 275-306
    • Whitcomb, J.M.1    Hughes, S.H.2
  • 2
    • 0027102597 scopus 로고
    • Genetics of retroviral integration
    • Goft, S. P. Genetics of retroviral integration. Annu. Rev. Genet 26, 527-544 (1992).
    • (1992) Annu. Rev. Genet , vol.26 , pp. 527-544
    • Goft, S.P.1
  • 3
    • 0027508068 scopus 로고
    • The human immunodeficiency virus integrase protein
    • Vink, C. & Plasterk, R.H.A. The human immunodeficiency virus integrase protein. Trends. Genet 9, 433-438 (1993).
    • (1993) Trends. Genet , vol.9 , pp. 433-438
    • Vink, C.1    Plasterk, R.H.A.2
  • 5
    • 0026330796 scopus 로고
    • HIV-1 DNA integration: Mechanism of viral DMA cleavage and DNA strand transfer
    • Engelman, A., Mizuuchi, K. S Craigie, R. HIV-1 DNA integration: mechanism of viral DMA cleavage and DNA strand transfer. Cell 67, 1211-1221(1991).
    • (1991) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.S.2    Craigie, R.3
  • 6
    • 0027456715 scopus 로고
    • Domains of integrase protein of human immunodeficiency virus type-1 responsible for polynucleotidyl transfer and zinc binding
    • Bushman, F. D., Engelman, A., Palmer, I., Wingfield, P.T. & Craigie, R. Domains of integrase protein of human immunodeficiency virus type-1 responsible for polynucleotidyl transfer and zinc binding. Proc. Natl. Acad. So. USA 90, 3428-3432 (1993).
    • (1993) Proc. Natl. Acad. So. USA , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Palmer, I.3    Wingfield, P.T.4    Craigie, R.5
  • 7
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus
    • Chow, S.A., Vincent, K.A., Ellison, V. & Brown, P.O. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science 255, 723-726(1992).
    • (1992) Science , vol.255 , pp. 723-726
    • Chow, S.A.1    Vincent, K.A.2    Ellison, V.3    Brown, P.O.4
  • 8
    • 0027210608 scopus 로고
    • Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein
    • . Vink, C., Oude Groeneger, A.M. & Plasterk, R.H.A. Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein. Nudele Adds Res. 21, 1419-1425 (1993).
    • (1993) Nudele Adds Res. , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude Groeneger, A.M.2    Plasterk, R.H.A.3
  • 10
    • 0027205243 scopus 로고
    • Characterization of a DNA binding domain in the C-terminus of HIV-1 integrase by deletion mutagenesis
    • Woerner, A.M. & Marcus-Sekura, CJ. Characterization of a DNA binding domain in the C-terminus of HIV-1 integrase by deletion mutagenesis. Nucleic Adds Res. 21, 3507-3511(1993).
    • (1993) Nucleic Adds Res. , vol.21 , pp. 3507-3511
    • Woerner, A.M.1    Marcus-Sekura, C.J.2
  • 11
    • 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. & Davies, D.R. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 266.1981-1986 (1994).
    • (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
  • 13
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase
    • Yang, W. & Steitz. T.A. Recombining the structures of HIV integrase, RuvC and RNase H. St/urture 3, 131-134(1995).
    • (1995) RuvC and RNase H. St/urture , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 18
    • 0029562273 scopus 로고
    • Characterization of the DNA-binding activity of HIV-1 integrase using a filter binding assay
    • Haugan, I.R., Nilsen, B.M., Worland. S.. Olsen, L. & Heiland, D.E. Characterization of the DNA-binding activity of HIV-1 integrase using a filter binding assay. Biochem. Biophys. Res. Commun. 217, 802-810 (1995).
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 802-810
    • Haugan, I.R.1    Nilsen, B.M.2    Worland, S.3    Olsen, L.4    Heiland, D.E.5
  • 19
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng, R., Jenkins, T.M. & Craigie, R. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc. Natl. Acad. Sei. U.S.A. 93, 13659-13664 (1996)
    • (1996) Proc. Natl. Acad. Sei. U.S.A. , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3
  • 20
    • 0027179694 scopus 로고
    • Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex
    • Engelman, A., Bushman, F.D. & Craigie, R. Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex. EMBQJ. 12, 3269-3275(1993).
    • (1993) EMBQJ. , vol.12 , pp. 3269-3275
    • Engelman, A.1    Bushman, F.D.2    Craigie, R.3
  • 21
    • 0027246609 scopus 로고
    • Complementation between HIV integrase proteins mutated in different domains
    • van Gent, D.C., Vink, C., Groeneger, A.A. & Plasterk, R.H.A. Complementation between HIV integrase proteins mutated in different domains. CMBO J. 12, 3261-3267(1993).
    • (1993) CMBO J. , vol.12 , pp. 3261-3267
    • Van Gent, D.C.1    Vink, C.2    Groeneger, A.A.3    Plasterk, R.H.A.4
  • 22
    • 0028888455 scopus 로고
    • An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active multimer
    • Ellison, V., Gerton, J., Vincent K.A. & Brown, P.O. An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active multimer. J. Biol. Chem. 270, 3320-3326 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 3320-3326
    • Ellison, V.1    Gerton, J.2    Vincent, K.A.3    Brown, P.O.4
  • 23
    • 0028097285 scopus 로고
    • Monoclonal antibodies against HIV type 1 integrase: Clues to molecular structure
    • Bizub-Bender, D., Kulkosky, J. & Skalka, A.M. Monoclonal antibodies against HIV type 1 integrase: clues to molecular structure. AIDS Research and Human RetroviruseslO, 1105-1115(1994).
    • (1994) AIDS Research and Human Retroviruses , vol.10 , pp. 1105-1115
    • Bizub-Bender, D.1    Kulkosky, J.2    Skalka, A.M.3
  • 24
    • 0025063347 scopus 로고
    • Analysis of backbone dynamics of interleukin-1β using two-dimensional inverse detected heteronuclear 15N-'H NMR spectroscopy
    • Clore, G.M., Driscoll, P.C., Wingfield, P.T. & Gronenborn, A.M. Analysis of backbone dynamics of interleukin-1β using two-dimensional inverse detected heteronuclear 15N-'H NMR spectroscopy. Biochemistry 29, 7387-7401 (1990).
    • (1990) Biochemistry , vol.29 , pp. 7387-7401
    • Clore, G.M.1    Driscoll, P.C.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 26
    • 0027456412 scopus 로고
    • Tautomeric states of the active-site histidines of phophorylated and unphophorylated IUGk, a signal transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques
    • Pelton, J.G., Torchia, D.A., Meadow, M.D. & Roseman, S. Tautomeric states of the active-site histidines of phophorylated and unphophorylated IUGk, a signal transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sd. 2, 543-558 (1993).
    • (1993) Protein Sd. , vol.2 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, M.D.3    Roseman, S.4
  • 27
    • 0025871254 scopus 로고
    • Structures of larger proteins in solution: Three- And four-dimensional heteronuclear NMR spectroscopy
    • Clore, G.M. & Gronenborn, A.M. Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science 252, 1390-1399 (1991).
    • (1991) Science , vol.252 , pp. 1390-1399
    • Clore, G.M.1    Gronenborn, A.M.2
  • 28
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax, A. & Grzesiek, 5. Methodological advances in protein NMR Acct Chem. Res. 26, 131-138(1993).
    • (1993) Acct Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek2
  • 29
    • 0028823713 scopus 로고
    • Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy
    • Gronenborn, A.M. S Clore, G.M. Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy. CRC Crit Rev. Biochem. Mol. Biol. 30, 351-385 (1995).
    • (1995) CRC Crit Rev. Biochem. Mol. Biol. , vol.30 , pp. 351-385
    • Gronenborn, A.M.S.1    Clore, G.M.2
  • 30
    • 0028673482 scopus 로고
    • Measurement of homo- And hetero-nuclear J couplings from quantitative J correlation
    • Bax, A. et al. Measurement of homo- and hetero-nuclear J couplings from quantitative J correlation. Meth. Enzymol. 239, 79-106 (1994).
    • (1994) Meth. Enzymol. , vol.239 , pp. 79-106
    • Bax, A.1
  • 31
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D. & McLaghlan, .D. Solvation energy in protein folding and binding. Wature319, 199-203(1986).
    • (1986) Wature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLaghlan, D.2
  • 32
    • 0029068108 scopus 로고    scopus 로고
    • Nuclear magnetic resonance characterization of the Jun Leucine zipper domain: Unusual properties of coiled-coil interfacial polar residues
    • Junius, F.K., MacKay, J.P.. Bubb, WA, Jensen, S.A., Weiss, MAS. & King, G.F. Nuclear magnetic resonance characterization of the Jun Leucine zipper domain: unusual properties of coiled-coil interfacial polar residues. Biochemistry, 6164-6174.
    • Biochemistry , pp. 6164-6174
    • Junius, F.K.1    MacKay, J.P.2    Bubb, W.A.3    Jensen, S.A.4    Weiss, M.A.S.5    King, G.F.6
  • 33
    • 0026035178 scopus 로고
    • Retroviral integrase domains: DNA binding and the recognition of LTR sequences
    • Khan, E., Mack, J.P.G, Katz, R.A., Kulkosky, J. & Skalka, A.M. Retroviral integrase domains: DNA binding and the recognition of LTR sequences. Nucl. Acids Res. 19, 851-860(1991).
    • (1991) Nucl. 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
  • 34
    • 33645888201 scopus 로고
    • Crystal structure of the trp repressor/operator complex at atomic resoution
    • Otwinowski Z. et al. Crystal structure of the trp repressor/operator complex at atomic resoution. Nature 335, 3321-329 (1988).
    • (1988) Nature , vol.335 , pp. 3321-3329
    • Otwinowski, Z.1
  • 35
    • 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., Rould, M.A., Jun, S.. Desplan, C. & Pabo, CO. 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).
    • (1995) Cell , vol.80 , pp. 639-650
    • Xu, W.1    Rould, M.A.2    Jun, S.3    Desplan, C.4    Pabo, C.O.5
  • 36
    • 0029127032 scopus 로고
    • Crystal structure of the site-specific recombinase y5 resolvase complexed with a 34 bp cleavage site
    • Yang, W. & Steitz, T.A. Crystal structure of the site-specific recombinase y5 resolvase complexed with a 34 bp cleavage site. Cell 82, 193-207 (1995).
    • (1995) Cell , vol.82 , pp. 193-207
    • Yang, W.1    Steitz, T.A.2
  • 37
    • 0029736725 scopus 로고    scopus 로고
    • Structure of the Escherlchia coli response regulator NarL
    • Baikalov, I. et al. Structure of the Escherlchia coli response regulator NarL Biochemistry 35, 11053-11061 (1996).
    • (1996) Biochemistry , vol.35 , pp. 11053-11061
    • Baikalov, I.1
  • 38
    • 0025188837 scopus 로고
    • Crystal structure of the engrailed homeodomain-DNA complex at 2.8 a resolution: A framework for understanding homeodomain-DNA interactions
    • Kissinger, C, Liu, B., Martin-Blanco, E., Kornberg, T. & Pabo, C.O. Crystal structure of the engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions. Cell 63.579-590 (1990).
    • (1990) Cell , vol.63 , pp. 579-590
    • Kissinger, C.1    Liu, B.2    Martin-Blanco, E.3    Kornberg, T.4    Pabo, C.O.5
  • 39
    • 0029980485 scopus 로고    scopus 로고
    • Soluble active mutant of HIV-1 integrase: Involvement of both the core and carboxyl-terminal domains in multimerization
    • Jenkins, T.M., Engelman, A., Ghirlando, R. & Craigie, R. A soluble active mutant of HIV-1 integrase: involvement of both the core and carboxyl-terminal domains in multimerization./ Blol. Chem. 271, 7712-7718(1996).
    • (1996) Blol. Chem. , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.A.4
  • 40
    • 0029017919 scopus 로고    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., Hickman, A.B., Dyda, F., Ghirlando, R., Davies, D.R. & Craigie, R. Catalytic domain of human immunodeficiency virus type 1 integrase: identification of a soluble mutant by systematic replacement of hydrophobic residues. Proc. Watl. Acad. Sei USA 92, 6057-6061.
    • Proc. Watl. Acad. Sei USA , vol.92 , pp. 6057-6061
    • Jenkins, T.M.1    Hickman, A.B.2    Dyda, F.3    Ghirlando, R.4    Davies, D.R.5    Craigie, R.6
  • 41
    • 85086809533 scopus 로고    scopus 로고
    • Heterogeneity in recombinant HIV-1 integrase corrected by site-directed mutagenesis: The identification and elimination of a protease cleavage site
    • In the press
    • Hickman, A.B., Dyda, F. & Craigie, R. Heterogeneity in recombinant HIV-1 integrase corrected by site-directed mutagenesis: the identification and elimination of a protease cleavage site. Prot Engng. 10, In the press.
    • Prot Engng. , vol.10
    • Hickman, A.B.1    Dyda, F.2    Craigie, R.3
  • 42
    • 0025043234 scopus 로고
    • Analysis of the junctions between human immunodeficiency virus type 1 proviral DNA and human DNA
    • Vink, C et al. Analysis of the junctions between human immunodeficiency virus type 1 proviral DNA and human DNA. J. Virol. 64, 5626-5627 (1990).
    • (1990) J. Virol. , vol.64 , pp. 5626-5627
    • Vink, C.1
  • 43
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and non-human cells transfected with an infectious molecular clone
    • Adachi, A. et al. Production of acquired immunodeficiency syndrome-associated retrovirus in human and non-human cells transfected with an infectious molecular clone../. Wot. 59.284-291 (1986).
    • (1986) ./. Wot. , vol.59 , pp. 284-291
    • Adachi, A.1
  • 44
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on U NIX pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on U NIX pipes. J. Biomolec. NMR 6, 277-293 (1995).
    • (1995) J. Biomolec. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 45
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two-, three- And four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett, D.S., Powers, R., Gronenborn, A.M. & Clore, G.M. A common sense approach to peak picking in two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Resort. 95, 214-220 (1991).
    • (1991) J. Magn. Resort. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 46
    • 0030981418 scopus 로고    scopus 로고
    • Two-dimensional NMR methods for determining xi angles of aromatic residues in proteins from thee-bond JCc, and JNc7 couplings
    • Hu, J.-S., Grzesiek, S. & Bax, A. Two-dimensional NMR methods for determining xi angles of aromatic residues in proteins from thee-bond JCc, and JNc7 couplings. J. Am. Chem. Soc. 119, 1803-1804(1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1803-1804
    • Hu, J.-S.1    Grzesiek, S.2    Bax, A.3
  • 47
    • 33847428924 scopus 로고    scopus 로고
    • 13C three-bond J couplings measured by three-dimensional heteronuclear NMR. how planar is the peptide bond
    • in the press
    • 13C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond. J. Am. Chem. Soc. in the press.
    • J. Am. Chem. Soc.
    • Hu, J.-S.1    Bax, A.2
  • 48
    • 0031111521 scopus 로고    scopus 로고
    • Ncγ couplings in isotopically enriched proteins
    • in press
    • Ncγ couplings in isotopically enriched proteins. J. Biomol. NMR in press (1997).
    • (1997) J. Biomol. NMR
    • Hu, J.-S.1    Bax, A.2
  • 49
    • 0029005929 scopus 로고
    • Rotational dynamics of calcium-free calmodulin studied by 1SN-NMR relaxation measurements, fur
    • Tjandra, N., Kuboniwa, H., Ren, H. & Bax, A. Rotational dynamics of calcium-free calmodulin studied by 1SN-NMR relaxation measurements, fur. J. Biochem. 230, 1014-1024(1995).
    • (1995) J. Biochem. , vol.230 , pp. 1014-1024
    • Tjandra, N.1    Kuboniwa, H.2    Ren, H.3    Bax, A.4
  • 50
    • 0027383637 scopus 로고
    • Calculational strategy for the structure determination of symmetric dimers by 'H NMR
    • Nilges, M. A calculational strategy for the structure determination of symmetric dimers by 'H NMR. Protems Struct. Funct Genet 17, 297-309 (1993).
    • (1993) Protems Struct. Funct Genet , vol.17 , pp. 297-309
    • Nilges, M.A.1
  • 51
    • 0025194652 scopus 로고
    • 'H-NMR stereospecific assignments by conformational database searches
    • Nilges, M., Clore, G.M. & Gronenborn, A.M. 'H-NMR stereospecific assignments by conformational database searches. BiopolymersiS, 813-822 (1990).
    • (1990) BiopolymersiS , pp. 813-822
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 52
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometrydynamical simulated annealing calculations
    • Nilges, M., Clore, G.M. S Gronenborn. A.M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometrydynamical simulated annealing calculations. FEES Lett 229, 317-324(1988).
    • (1988) FEES Lett , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.S.2    Gronenborn, A.M.3
  • 54
    • 0028432974 scopus 로고
    • The impact of direct refinement against three-bond HN-CαH coupling constants on protein structure determination by NMR
    • Garrett, D.S. et al. The impact of direct refinement against three-bond HN-CαH coupling constants on protein structure determination by NMR. J. Magn. Reson. SeriesB 104, 99-103 (1994).
    • (1994) J. Magn. Reson. SeriesB , vol.104 , pp. 99-103
    • Garrett, D.S.1
  • 56
    • 0030000912 scopus 로고    scopus 로고
    • Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases
    • Kuszewski, J., Gronenborn. A.M. & Clore, G.M. Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Prot. Sei. 5, 1067-1080 (1996).
    • (1996) Prot. Sei. , vol.5 , pp. 1067-1080
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 57
    • 0031083293 scopus 로고    scopus 로고
    • Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids
    • Kuszewski, J., Gronenborn, A.M. & Clore, G.M. Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. J. Magn. Reson. 125, 171-177 (1997).
    • (1997) J. Magn. Reson. , vol.125 , pp. 171-177
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 58
    • 0030621858 scopus 로고    scopus 로고
    • Torsion-angle molecular dynamics as a new efficient tool for NMRstructure calculation
    • Stein, E.G., Rice, L.M. & Brünger, A.T. Torsion-angle molecular dynamics as a new efficient tool for NMRstructure calculation./Magn. Reson. 124, 154-164(1997).
    • (1997) /Magn. Reson. , vol.124 , pp. 154-164
    • Stein, E.G.1    Rice, L.M.2    Brünger, A.T.3
  • 59
    • 0023998438 scopus 로고
    • Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints: Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2
    • Nilges, M, Gronenborn, A.M., Brünger, A.T. & Clore, G.M. Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints: application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Prot Engng. 2, 27-38 (1988).
    • (1988) Prot Engng. , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brünger, A.T.3    Clore, G.M.4
  • 60
    • 0025110477 scopus 로고
    • High resolution three-dimensional solution structure of a single zinc finger from a human enhancer binding protein in solution
    • Omichinski, J., Clore, G.M., Appella, E., Sakaguchi, K. & Gronenborn, A.M. High resolution three-dimensional solution structure of a single zinc finger from a human enhancer binding protein in solution. Biochemistry 29, 9324-9334. (1990).
    • (1990) Biochemistry , vol.29 , pp. 9324-9334
    • Omichinski, J.1    Clore, G.M.2    Appella, E.3    Sakaguchi, K.4    Gronenborn, A.M.5
  • 61
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R, Billeter, M. & Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 52-55 (1996).
    • (1996) J. Mol. Graphics , vol.14 , pp. 52-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 62
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig. B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct Genet 11, 281-296 (1991).
    • (1991) Proteins Struct. Funct Genet 11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 64
    • 84986512474 scopus 로고
    • CHARMM: A program for macromolecular energy minimization and dynamics calculations
    • Brooks, B.R. et al. CHARMM: a program for macromolecular energy minimization and dynamics calculations./ Comput. Chem. 4, 187-217 (1993).
    • (1993) / Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.