메뉴 건너뛰기




Volumn 17, Issue 12, 2009, Pages 1625-1635

Structure of HIV-1 Reverse Transcriptase with the Inhibitor β-Thujaplicinol Bound at the RNase H Active Site

Author keywords

MICROBIO; PROTEINS; RNA

Indexed keywords

BETA THUJAPLICINOL; NUCLEOTIDYLTRANSFERASE INHIBITOR; RIBONUCLEASE H; RNA DIRECTED DNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 71049185147     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.09.016     Document Type: Article
Times cited : (131)

References (55)
  • 2
    • 64649098298 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase can simultaneously engage its DNA/RNA substrate at both DNA polymerase and RNase H active sites: implications for RNase H inhibition
    • Beilhartz G.L., Wendeler M., Baichoo N., Rausch J., Le Grice S., and Gotte M. HIV-1 reverse transcriptase can simultaneously engage its DNA/RNA substrate at both DNA polymerase and RNase H active sites: implications for RNase H inhibition. J. Mol. Biol. 388 (2009) 462-474
    • (2009) J. Mol. Biol. , vol.388 , pp. 462-474
    • Beilhartz, G.L.1    Wendeler, M.2    Baichoo, N.3    Rausch, J.4    Le Grice, S.5    Gotte, M.6
  • 3
    • 13044301434 scopus 로고
    • Ground state structures of heptafulvene π-systems
    • Nozoe T., Breslow R., Itô S., Hafner K., and Murata I. (Eds), John Wiley & Sons, Inc., New York
    • Bertelli D.J. Ground state structures of heptafulvene π-systems. In: Nozoe T., Breslow R., Itô S., Hafner K., and Murata I. (Eds). Topics in Nonbenzenoid Aromatic Chemistry Volume 1 (1973), John Wiley & Sons, Inc., New York 29-46
    • (1973) Topics in Nonbenzenoid Aromatic Chemistry , vol.1 , pp. 29-46
    • Bertelli, D.J.1
  • 4
    • 33846148366 scopus 로고    scopus 로고
    • Economical parallel protein expression screening and scale-up in Escherichia coli
    • Brodsky O., and Cronin C.N. Economical parallel protein expression screening and scale-up in Escherichia coli. J. Struct. Funct. Genomics 7 (2006) 101-108
    • (2006) J. Struct. Funct. Genomics , vol.7 , pp. 101-108
    • Brodsky, O.1    Cronin, C.N.2
  • 7
    • 0028806233 scopus 로고
    • Crystallization of human immunodeficiency virus type 1 reverse transcriptase with and without nucleic acid substrates, inhibitors and an antibody fab fragment
    • Clark Jr. A.D., Jacobo-Molina A., Clark P., Hughes S.H., and Arnold E. Crystallization of human immunodeficiency virus type 1 reverse transcriptase with and without nucleic acid substrates, inhibitors and an antibody fab fragment. Methods Enzymol. 262 (1995) 171-185
    • (1995) Methods Enzymol. , vol.262 , pp. 171-185
    • Clark Jr., A.D.1    Jacobo-Molina, A.2    Clark, P.3    Hughes, S.H.4    Arnold, E.5
  • 8
    • 0017075905 scopus 로고
    • Binding affinities of retinol and related compounds to retinol binding proteins
    • Cogan U., Kopelman M., Mokady S., and Shinitzky M. Binding affinities of retinol and related compounds to retinol binding proteins. Eur. J. Biochem. 65 (1976) 71-78
    • (1976) Eur. J. Biochem. , vol.65 , pp. 71-78
    • Cogan, U.1    Kopelman, M.2    Mokady, S.3    Shinitzky, M.4
  • 9
    • 0025908083 scopus 로고
    • Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
    • Davies II J.F., Hostomska Z., Hostomsky Z., Jordan S.R., and Matthews D.A. Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science 252 (1991) 88-95
    • (1991) Science , vol.252 , pp. 88-95
    • Davies II, J.F.1    Hostomska, Z.2    Hostomsky, Z.3    Jordan, S.R.4    Matthews, D.A.5
  • 10
    • 0002985035 scopus 로고
    • Structure of stipitatic acid
    • Dewar M.J.S. Structure of stipitatic acid. Nature 155 (1945) 50-51
    • (1945) Nature , vol.155 , pp. 50-51
    • Dewar, M.J.S.1
  • 11
    • 0030786006 scopus 로고    scopus 로고
    • Protein-nucleic acid interactions and DNA conformation in a complex of human immunodeficiency virus type 1 reverse transcriptase with a double-stranded DNA template-primer
    • Ding J., Hughes S.H., and Arnold E. Protein-nucleic acid interactions and DNA conformation in a complex of human immunodeficiency virus type 1 reverse transcriptase with a double-stranded DNA template-primer. Biopolymers 44 (1997) 125-138
    • (1997) Biopolymers , vol.44 , pp. 125-138
    • Ding, J.1    Hughes, S.H.2    Arnold, E.3
  • 13
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for x-ray protein structure refinement
    • Engh R.A., and Huber R. Accurate bond and angle parameters for x-ray protein structure refinement. Acta Crystallogr. A 47 (1991) 392-400
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 14
    • 0006167042 scopus 로고
    • Occurrence of 2,7-dihydroxy-4-isopropyl-2,4,6-cycloheptatrien-1-one (7-hydroxy-4-iso-propyltropolone) in Western Red Cedar (Thuja plicata Donn.)
    • Gardner J.A.F., Baron G.M., and MacLean H. Occurrence of 2,7-dihydroxy-4-isopropyl-2,4,6-cycloheptatrien-1-one (7-hydroxy-4-iso-propyltropolone) in Western Red Cedar (Thuja plicata Donn.). Can. J. Chem. 35 (1957) 1039-1048
    • (1957) Can. J. Chem. , vol.35 , pp. 1039-1048
    • Gardner, J.A.F.1    Baron, G.M.2    MacLean, H.3
  • 16
    • 0035831544 scopus 로고    scopus 로고
    • Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site
    • Goedken E.R., and Marqusee S. Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site. J. Biol. Chem. 276 (2001) 7266-7271
    • (2001) J. Biol. Chem. , vol.276 , pp. 7266-7271
    • Goedken, E.R.1    Marqusee, S.2
  • 20
    • 0030586090 scopus 로고    scopus 로고
    • Structure of unliganded HIV-1 reverse transcriptase at 2.7 Å resolution: implications of conformational changes for polymerization and inhibition mechanisms
    • Hsiou Y., Ding J., Das K., Clark-Jr A.D., Hughes S.H., and Arnold E. Structure of unliganded HIV-1 reverse transcriptase at 2.7 Å resolution: implications of conformational changes for polymerization and inhibition mechanisms. Structure 4 (1996) 853-860
    • (1996) Structure , vol.4 , pp. 853-860
    • Hsiou, Y.1    Ding, J.2    Das, K.3    Clark-Jr, A.D.4    Hughes, S.H.5    Arnold, E.6
  • 21
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance
    • Huang H., Chopra R., Verdine G.L., and Harrison S.C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282 (1998) 1669-1675
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 23
    • 84889120137 scopus 로고
    • Improved experimental procedures for building protein 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. Improved experimental procedures for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0030460727 scopus 로고    scopus 로고
    • Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion: proposal of a novel catalytic role for Glu48
    • Kanaya S., Oobatake M., and Liu Y. Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion: proposal of a novel catalytic role for Glu48. J. Biol. Chem. 271 (1996) 32729-32736
    • (1996) J. Biol. Chem. , vol.271 , pp. 32729-32736
    • Kanaya, S.1    Oobatake, M.2    Liu, Y.3
  • 25
    • 0027377121 scopus 로고
    • Crystal structure of Escherichia coli Rnase HI in complex with Mg2+ at 2.8 A resolution: proof for a single Mg(2+)-binding site
    • Katayanagi K., Okumura M., and Morikawa K. Crystal structure of Escherichia coli Rnase HI in complex with Mg2+ at 2.8 A resolution: proof for a single Mg(2+)-binding site. Proteins 17 (1993) 337-346
    • (1993) Proteins , vol.17 , pp. 337-346
    • Katayanagi, K.1    Okumura, M.2    Morikawa, K.3
  • 26
    • 0032545251 scopus 로고    scopus 로고
    • Activation/attenuation model for RNase H: a one-metal mechanism with second-metal inhibition
    • Keck J.L., Goedken E.R., and Marqusee S. Activation/attenuation model for RNase H: a one-metal mechanism with second-metal inhibition. J. Biol. Chem. 273 (1998) 34128-34133
    • (1998) J. Biol. Chem. , vol.273 , pp. 34128-34133
    • Keck, J.L.1    Goedken, E.R.2    Marqusee, S.3
  • 27
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: applications of the free R value
    • Kleywegt G.J., and Brünger A.T. Checking your imagination: applications of the free R value. Structure 4 (1996) 897-904
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 28
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • Kleywegt G.J., Bergfors T., Senn H., LeMotte P., Gsell B., Shudo K., and Jones T.A. Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 2 (1994) 1241-1258
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    LeMotte, P.4    Gsell, B.5    Shudo, K.6    Jones, T.A.7
  • 29
    • 33646497669 scopus 로고    scopus 로고
    • Recent progress in the design of small molecule inhibitors of HIV RNase H
    • Klumpp K., and Mirzadegan T. Recent progress in the design of small molecule inhibitors of HIV RNase H. Curr. Pharm. Des. 12 (2006) 1909-1922
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 1909-1922
    • Klumpp, K.1    Mirzadegan, T.2
  • 31
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt L.A., Wang J., Friedman J.M., Rice P.A., and Steitz T.A. Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256 (1992) 1783-1790
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 32
    • 0347366871 scopus 로고
    • Advances in the chemistry of the tropylium ion
    • Kolomnikova G.D., and Parnes Z.N. Advances in the chemistry of the tropylium ion. Russ. Chem. Rev. 36 (1967) 735-753
    • (1967) Russ. Chem. Rev. , vol.36 , pp. 735-753
    • Kolomnikova, G.D.1    Parnes, Z.N.2
  • 33
    • 17644371341 scopus 로고    scopus 로고
    • Exosite-driven substrate specificity and function in coagulation
    • Krishnaswamy S. Exosite-driven substrate specificity and function in coagulation. J. Thromb. Haemost. 3 (2005) 54-67
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 54-67
    • Krishnaswamy, S.1
  • 34
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structure cristallines
    • Luzzati V. Traitement statistique des erreurs dans la determination des structure cristallines. Acta Crystallogr. 5 (1952) 802-810
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 37
    • 21244451435 scopus 로고    scopus 로고
    • Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis
    • Nowotny M., Gaidamakov S.A., Crouch R.J., and Yang W. Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis. Cell 121 (2005) 1005-1016
    • (2005) Cell , vol.121 , pp. 1005-1016
    • Nowotny, M.1    Gaidamakov, S.A.2    Crouch, R.J.3    Yang, W.4
  • 38
    • 35348978302 scopus 로고    scopus 로고
    • Structure of Human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription
    • Nowotny M., Gaidamakov S.A., Ghirlando R., Cerritelli S.M., Crouch R.J., and Yang W. Structure of Human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription. Mol. Cell 28 (2007) 264-276
    • (2007) Mol. Cell , vol.28 , pp. 264-276
    • Nowotny, M.1    Gaidamakov, S.A.2    Ghirlando, R.3    Cerritelli, S.M.4    Crouch, R.J.5    Yang, W.6
  • 39
    • 0026225732 scopus 로고
    • Binding of metal ions to E. Coli RNase HI observed by 1H-15N heteronuclear 2D NMR
    • Oda Y., Nakamura H., Kanaya S., and Ikehara M. Binding of metal ions to E. Coli RNase HI observed by 1H-15N heteronuclear 2D NMR. J. Biomol. NMR 1 (1991) 247-255
    • (1991) J. Biomol. NMR , vol.1 , pp. 247-255
    • Oda, Y.1    Nakamura, H.2    Kanaya, S.3    Ikehara, M.4
  • 40
    • 0027472170 scopus 로고
    • Role of histidine 124 in the catalytic function of ribonuclease HI From Escherichia coli
    • Oda Y., Yoshida M., and Kanaya S. Role of histidine 124 in the catalytic function of ribonuclease HI From Escherichia coli. J. Biol. Chem. 268 (1993) 88-92
    • (1993) J. Biol. Chem. , vol.268 , pp. 88-92
    • Oda, Y.1    Yoshida, M.2    Kanaya, S.3
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Carter J.C.W., and Sweet R.M. (Eds), Academic Press, New York
    • Otwinowski Z., and Minor W. Processing of x-ray diffraction data collected in oscillation mode. In: Carter J.C.W., and Sweet R.M. (Eds). Macromolecular Crystallography Part A Volume 276 (1997), Academic Press, New York 307-326
    • (1997) Macromolecular Crystallography Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0037905523 scopus 로고    scopus 로고
    • DENZO and SCALEPACK
    • Rossmann M.G., and Arnold E. (Eds), Kluwer Academic Publishers, Boston
    • Otwinowski Z., and Minor W. DENZO and SCALEPACK. In: Rossmann M.G., and Arnold E. (Eds). Crystallography of Biological Macromolecules Volume F (2001), Kluwer Academic Publishers, Boston 226-235
    • (2001) Crystallography of Biological Macromolecules , vol.F , pp. 226-235
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0141758137 scopus 로고    scopus 로고
    • A fluorescence-based high-throughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity
    • Parniak M.A., Min K.L., Budihas S.R., Le Grice S.F., and Beutler J.A. A fluorescence-based high-throughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity. Anal. Biochem. 322 (2003) 33-39
    • (2003) Anal. Biochem. , vol.322 , pp. 33-39
    • Parniak, M.A.1    Min, K.L.2    Budihas, S.R.3    Le Grice, S.F.4    Beutler, J.A.5
  • 44
    • 0002407748 scopus 로고
    • Tropones and tropolones
    • Pauson P.L. Tropones and tropolones. Chem. Rev. 55 (1955) 9-136
    • (1955) Chem. Rev. , vol.55 , pp. 9-136
    • Pauson, P.L.1
  • 45
    • 0000001557 scopus 로고
    • Seven-membered conjugated carbo- and heterocyclic compounds and their homoconjugated analogs and metal complexes: synthesis, biosynthesis, structure, and reactivity
    • Pietra F. Seven-membered conjugated carbo- and heterocyclic compounds and their homoconjugated analogs and metal complexes: synthesis, biosynthesis, structure, and reactivity. Chem. Rev. 73 (1973) 293-364
    • (1973) Chem. Rev. , vol.73 , pp. 293-364
    • Pietra, F.1
  • 46
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1373-1382
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 48
    • 9944232661 scopus 로고    scopus 로고
    • Taking aim at a moving target: designing drugs to inhibit drug-resistant HIV-1 reverse transcriptases
    • Sarafianos S.G., Das K., Hughes S.H., and Arnold E. Taking aim at a moving target: designing drugs to inhibit drug-resistant HIV-1 reverse transcriptases. Curr. Opin. Struct. Biol. 14 (2004) 716-730
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 716-730
    • Sarafianos, S.G.1    Das, K.2    Hughes, S.H.3    Arnold, E.4
  • 50
    • 0001851755 scopus 로고
    • Inactivation of the RNaseH domain of HIV-1 reverse transcriptase blocks viral infectivity
    • Papas T. (Ed), Portfolio Publishing Company, Houston, TX
    • Schatz O., Cromme F., Naas T., Lindermann D., Gruninger-Leitch F., Mous J., and Le Grice S.F.J. Inactivation of the RNaseH domain of HIV-1 reverse transcriptase blocks viral infectivity. In: Papas T. (Ed). Oncogenesis and AIDS (1990), Portfolio Publishing Company, Houston, TX 55-68
    • (1990) Oncogenesis and AIDS , pp. 55-68
    • Schatz, O.1    Cromme, F.2    Naas, T.3    Lindermann, D.4    Gruninger-Leitch, F.5    Mous, J.6    Le Grice, S.F.J.7
  • 52
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz T.A., and Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl. Acad. Sci. USA 90 (1993) 6498-6502
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 53
    • 0026056935 scopus 로고
    • Mutations within the RNase H domain of HIV-1 RT abolish virus infectivity
    • Tisdale M., Schulze T., Larder B.A., and Moelling K. Mutations within the RNase H domain of HIV-1 RT abolish virus infectivity. J. Gen. Virol. 72 (1991) 59-66
    • (1991) J. Gen. Virol. , vol.72 , pp. 59-66
    • Tisdale, M.1    Schulze, T.2    Larder, B.A.3    Moelling, K.4
  • 55
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein
    • Yang W., Hendrickson W.A., Crouch R.J., and Satow Y. Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein. Science 249 (1990) 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.