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Volumn 78, Issue 3, 2009, Pages 224-230

Distinct interactions of 2′- and 3′-O-(N-methyl)anthraniloyl-isomers of ATP and GTP with the adenylyl cyclase toxin of Bacillus anthracis, edema factor

Author keywords

Calmodulin; Edema factor; Fluorescence spectroscopy; MANT nucleotide; Molecular modelling

Indexed keywords

2' O (N METHYL)ANTHRANILOYL 3' DEOXY ADENOSINE TRIPHOSPHATE; 3' O (N METHYL)ANTHRANILOYL 2' DEOXY ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE TOXIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 67349287667     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2009.04.006     Document Type: Article
Times cited : (11)

References (24)
  • 1
    • 0036428851 scopus 로고    scopus 로고
    • The structure and function of novel proteins of Bacillus anthracis and other spore-forming bacteria: development of novel prophylactic and therapeutic agents
    • Jedrzejas M.J. The structure and function of novel proteins of Bacillus anthracis and other spore-forming bacteria: development of novel prophylactic and therapeutic agents. Crit Rev Biochem Mol Biol 37 (2002) 339-373
    • (2002) Crit Rev Biochem Mol Biol , vol.37 , pp. 339-373
    • Jedrzejas, M.J.1
  • 2
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • Drum C.L., Yan S.Z., Bard J., Shen Y.Q., Lu D., Soelaiman S., et al. Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415 (2002) 396-402
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.L.1    Yan, S.Z.2    Bard, J.3    Shen, Y.Q.4    Lu, D.5    Soelaiman, S.6
  • 3
    • 12244306922 scopus 로고    scopus 로고
    • Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins
    • Shen Y., Lee Y.S., Soelaiman S., Bergson P., Lu D., Chen A., et al. Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins. EMBO J 21 (2002) 6721-6732
    • (2002) EMBO J , vol.21 , pp. 6721-6732
    • Shen, Y.1    Lee, Y.S.2    Soelaiman, S.3    Bergson, P.4    Lu, D.5    Chen, A.6
  • 4
    • 1542327666 scopus 로고    scopus 로고
    • Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection
    • Shen Y., Zhukovskaya N.L., Zimmer M.I., Soelaiman S., Bergson P., Wang C.R., et al. Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection. Proc Natl Acad Sci USA 101 (2004) 3242-3247
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3242-3247
    • Shen, Y.1    Zhukovskaya, N.L.2    Zimmer, M.I.3    Soelaiman, S.4    Bergson, P.5    Wang, C.R.6
  • 5
    • 62149085232 scopus 로고    scopus 로고
    • Molecular analysis of the interaction of anthrax adenylyl cyclase toxin, edema factor, with 2′(3′)-O-(N-(methyl)anthraniloyl)-substituted purine and pyrimidine nucleotides
    • Taha H.M., Schmidt J., Göttle M., Suryanarayana S., Shen Y., Tang W.J., et al. Molecular analysis of the interaction of anthrax adenylyl cyclase toxin, edema factor, with 2′(3′)-O-(N-(methyl)anthraniloyl)-substituted purine and pyrimidine nucleotides. Mol Pharmacol 75 (2009) 693-703
    • (2009) Mol Pharmacol , vol.75 , pp. 693-703
    • Taha, H.M.1    Schmidt, J.2    Göttle, M.3    Suryanarayana, S.4    Shen, Y.5    Tang, W.J.6
  • 6
    • 2442506761 scopus 로고    scopus 로고
    • Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides
    • Gille A., Lushington G.H., Mou T.C., Doughty M.B., Johnson R.A., and Seifert R. Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides. J Biol Chem 279 (2004) 19955-19969
    • (2004) J Biol Chem , vol.279 , pp. 19955-19969
    • Gille, A.1    Lushington, G.H.2    Mou, T.C.3    Doughty, M.B.4    Johnson, R.A.5    Seifert, R.6
  • 7
    • 0037630420 scopus 로고    scopus 로고
    • 2′(3′)-O-(N-methylanthraniloyl)-substituted GTP analogs: a novel class of potent competitive adenylyl cyclase inhibitors
    • Gille A., and Seifert R. 2′(3′)-O-(N-methylanthraniloyl)-substituted GTP analogs: a novel class of potent competitive adenylyl cyclase inhibitors. J Biol Chem 278 (2003) 12672-12679
    • (2003) J Biol Chem , vol.278 , pp. 12672-12679
    • Gille, A.1    Seifert, R.2
  • 8
    • 14844299755 scopus 로고    scopus 로고
    • Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2′(3′)-O-(N-methylanthraniloyl)-guanosine 5′-triphosphate
    • Mou T.C., Gille A., Fancy D.A., Seifert R., and Sprang S.R. Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2′(3′)-O-(N-methylanthraniloyl)-guanosine 5′-triphosphate. J Biol Chem 280 (2005) 7253-7261
    • (2005) J Biol Chem , vol.280 , pp. 7253-7261
    • Mou, T.C.1    Gille, A.2    Fancy, D.A.3    Seifert, R.4    Sprang, S.R.5
  • 9
    • 33747624168 scopus 로고    scopus 로고
    • Broad specificity of mammalian adenylyl cyclase for interaction with 2′,3′-substituted purine- and pyrimidine-nucleotide inhibitors
    • Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., and Sprang S.R. Broad specificity of mammalian adenylyl cyclase for interaction with 2′,3′-substituted purine- and pyrimidine-nucleotide inhibitors. Mol Pharmacol 70 (2006) 878-886
    • (2006) Mol Pharmacol , vol.70 , pp. 878-886
    • Mou, T.C.1    Gille, A.2    Suryanarayana, S.3    Richter, M.4    Seifert, R.5    Sprang, S.R.6
  • 10
    • 0030971247 scopus 로고    scopus 로고
    • Fluorescent nucleotide analogs: synthesis and applications
    • Jameson D.M., and Eccleston J.F. Fluorescent nucleotide analogs: synthesis and applications. Methods Enzymol 278 (1997) 363-390
    • (1997) Methods Enzymol , vol.278 , pp. 363-390
    • Jameson, D.M.1    Eccleston, J.F.2
  • 11
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka T. New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim Biophys Acta 742 (1983) 496-508
    • (1983) Biochim Biophys Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 12
    • 36549053591 scopus 로고    scopus 로고
    • The Tripos Associates, St. Louis, MO, USA
    • SYBYL 7.2 (2006), The Tripos Associates, St. Louis, MO, USA
    • (2006) SYBYL 7.2
  • 13
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity: a rapid access to atomic charges
    • Gasteiger J., and Marsili M. Iterative partial equalization of orbital electronegativity: a rapid access to atomic charges. Tetrahedron 36 (1980) 3219-3228
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 14
    • 84988115618 scopus 로고
    • Validation of the general purpose Tripos 5.2 force field
    • Clark M., Cramer III R.D., and Van Opdenbosch N. Validation of the general purpose Tripos 5.2 force field. J Comput Chem 10 (1989) 982-1012
    • (1989) J Comput Chem , vol.10 , pp. 982-1012
    • Clark, M.1    Cramer III, R.D.2    Van Opdenbosch, N.3
  • 15
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey M., Kramer B., Lengauer T., and Klebe G.A. A fast flexible docking method using an incremental construction algorithm. J Mol Biol 261 (1996) 470-489
    • (1996) J Mol Biol , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.A.4
  • 16
    • 0029000922 scopus 로고
    • Prediction of drug binding affinities by comparative binding energy analysis
    • Ortiz A.R., Pisabarro M.T., Gago F., and Wade R.C. Prediction of drug binding affinities by comparative binding energy analysis. J Med Chem 38 (1995) 2681-2691
    • (1995) J Med Chem , vol.38 , pp. 2681-2691
    • Ortiz, A.R.1    Pisabarro, M.T.2    Gago, F.3    Wade, R.C.4
  • 19
    • 34548315751 scopus 로고    scopus 로고
    • Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides
    • Göttle M., Dove S., Steindel P., Shen Y., Tang W.J., Geduhn J., et al. Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides. Mol Pharmacol 72 (2007) 526-535
    • (2007) Mol Pharmacol , vol.72 , pp. 526-535
    • Göttle, M.1    Dove, S.2    Steindel, P.3    Shen, Y.4    Tang, W.J.5    Geduhn, J.6
  • 22
    • 49049101073 scopus 로고    scopus 로고
    • A fluorimetric assay for real-time monitoring of adenylyl cyclase activity based on terbium norfloxacin
    • Spangler C.M., Spangler C., Göttle M., Shen Y., Tang W.J., Seifert R., et al. A fluorimetric assay for real-time monitoring of adenylyl cyclase activity based on terbium norfloxacin. Anal Biochem 381 (2008) 86-93
    • (2008) Anal Biochem , vol.381 , pp. 86-93
    • Spangler, C.M.1    Spangler, C.2    Göttle, M.3    Shen, Y.4    Tang, W.J.5    Seifert, R.6
  • 23
    • 0026349335 scopus 로고
    • Is there a rate-limiting step before GTP cleavage by H-ras p21?
    • Rensland H., Lautwein A., Wittinghofer A., and Goody R.S. Is there a rate-limiting step before GTP cleavage by H-ras p21?. Biochemistry 30 (1991) 11181-11185
    • (1991) Biochemistry , vol.30 , pp. 11181-11185
    • Rensland, H.1    Lautwein, A.2    Wittinghofer, A.3    Goody, R.S.4
  • 24
    • 0027297116 scopus 로고
    • N-ras catalyzed by GAP: studies with a fluorescent GTP analogue
    • N-ras catalyzed by GAP: studies with a fluorescent GTP analogue. Biochemistry 32 (1993) 7451-7459
    • (1993) Biochemistry , vol.32 , pp. 7451-7459
    • Moore, K.J.M.1    Webb, M.R.2    Eccleston, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.