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Volumn 287, Issue 16, 2012, Pages 12893-12903

Aminoglycoside 2″-phosphotransferase IIIa (APH(2″)-IIIa) prefers GTP over ATP: Structural templates for nucleotide recognition in the bacterial aminoglycoside-2″ kinases

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDES; ANTIBIOTIC RESISTANCE; ATP-BINDING; COFACTORS; EUKARYOTIC PROTEINS; GTP BINDING; KINASE FAMILY; PHOSPHOTRANSFERASES; PROTEIN KINASE; SINGLE NUCLEOTIDES; STRUCTURAL DETERMINANTS; STRUCTURAL TEMPLATES; TYROSINE RESIDUES;

EID: 84859747165     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.341206     Document Type: Article
Times cited : (22)

References (57)
  • 1
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • DOI 10.1038/327389a0
    • Moazed, D., and Noller, H. F. (1987) Interaction of antibiotics with functional sites in 16 S ribosomal RNA. Nature 327, 389-394 (Pubitemid 17075811)
    • (1987) Nature , vol.327 , Issue.6121 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 2
    • 0027988447 scopus 로고
    • Dissociation rate of cognate peptidyl-tRNA from the A-site of hyper-accurate and error-prone ribosomes
    • DOI 10.1111/j.1432-1033.1994.tb20059.x
    • Karimi, R., and Ehrenberg, M. (1994) Dissociation rate of cognate peptidyl-tRNA from the A-site of hyper-accurate and error-prone ribosomes. Eur. J. Biochem. 226, 355-360 (Pubitemid 24379053)
    • (1994) European Journal of Biochemistry , vol.226 , Issue.2 , pp. 355-360
    • Karimi, R.1    Ehrenberg, M.2
  • 3
    • 33750976354 scopus 로고    scopus 로고
    • Molecular Contacts Between Antibiotics and the 30S Ribosomal Particle
    • DOI 10.1016/S0076-6879(06)15012-0, PII S0076687906150120, Glycobiology
    • Wirmer, J., and Westhof, E. (2006) Molecular contacts between antibiotics and the 30 S ribosomal particle. Methods Enzymol. 415, 180-202 (Pubitemid 44751098)
    • (2006) Methods in Enzymology , vol.415 , pp. 180-202
    • Wirmer, J.1    Westhof, E.2
  • 5
    • 0032614298 scopus 로고    scopus 로고
    • Aminoglycoside phosphotransferases: Proteins, structure and mechanism
    • Wright, G. D., and Thompson, P. R. (1999) Aminoglycoside phosphotransferases: proteins, structure and mechanism. Front. Biosci. 4, D9-21
    • (1999) Front. Biosci. , vol.4
    • Wright, G.D.1    Thompson, P.R.2
  • 6
    • 0032828903 scopus 로고    scopus 로고
    • Aminoglycoside-modifying enzymes
    • Wright, G. D. (1999) Aminoglycoside-modifying enzymes. Curr. Opin. Microbiol. 2, 499-503
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 499-503
    • Wright, G.D.1
  • 7
    • 0035986724 scopus 로고    scopus 로고
    • Aminoglycoside antibiotic resistance by enzymatic deactivation
    • DOI 10.2174/1568005023342533
    • Smith, C. A., and Baker, E. N. (2002) Aminoglycoside antibiotic resistance by enzymatic deactivation. Curr. Drug Targets Infect. Disord. 2, 143-160 (Pubitemid 34649862)
    • (2002) Current Drug Targets - Infectious Disorders , vol.2 , Issue.2 , pp. 143-160
    • Smith, C.A.1    Baker, E.N.2
  • 8
    • 0037770202 scopus 로고    scopus 로고
    • Versatility of aminoglycosides and prospects for their future
    • DOI 10.1128/CMR.16.3.430-450.2003
    • Vakulenko, S. B., and Mobashery, S. (2003) Versatility of aminoglycosides and prospects for their future. Clin. Microbiol. Rev. 16, 430-450 (Pubitemid 36871315)
    • (2003) Clinical Microbiology Reviews , vol.16 , Issue.3 , pp. 430-450
    • Vakulenko, S.B.1    Mobashery, S.2
  • 10
    • 18844441171 scopus 로고    scopus 로고
    • Phosphoryl transfer by aminoglycoside 3′-phosphotransferases and manifestation of antibiotic resistance
    • DOI 10.1016/j.bioorg.2004.11.001, PII S0045206804000951, Mechanistic Enzymology
    • Kim, C., and Mobashery, S. (2005) Phosphoryl transfer by aminoglycoside 3′-phosphotransferases and manifestation of antibiotic resistance. Bioorg. Chem. 33, 149-158 (Pubitemid 40693277)
    • (2005) Bioorganic Chemistry , vol.33 , Issue.3 , pp. 149-158
    • Kim, C.1    Mobashery, S.2
  • 11
    • 0043023392 scopus 로고    scopus 로고
    • The role of the putative catalytic base in the phosphoryl transfer reaction in a protein kinase: First-principles calculations
    • DOI 10.1021/ja029618u
    • Valiev, M., Kawai, R., Adams, J. A., and Weare, J. H. (2003) The role of the putative catalytic base in the phosphoryl transfer reaction in a protein kinase. First-principles calculations. J. Am. Chem. Soc. 125, 9926-9927 (Pubitemid 36994914)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.33 , pp. 9926-9927
    • Valiev, M.1    Kawai, R.2    Adams, J.A.3    Weare, J.H.4
  • 12
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases. Evolution of dynamic regulatory proteins
    • Taylor, S. S., and Kornev, A. P. (2011) Protein kinases. Evolution of dynamic regulatory proteins. Trends Biochem. Sci. 36, 65-77
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 13
    • 0031722706 scopus 로고    scopus 로고
    • Novel families of putative protein kinases in bacteria and archaea: Evolution of the 'eukaryotic' protein kinase superfamily
    • Leonard, C. J., Aravind, L., and Koonin, E. V. (1998) Novel families of putative protein kinases in bacteria and archaea. Evolution of the "eukaryotic" protein kinase superfamily. Genome Res. 8, 1038-1047 (Pubitemid 28532492)
    • (1998) Genome Research , vol.8 , Issue.10 , pp. 1038-1047
    • Leonard, C.J.1    Aravind, L.2    Koonin, E.V.3
  • 14
    • 79952426399 scopus 로고    scopus 로고
    • Eukaryote-like serine/threonine kinases and phosphatases in bacteria
    • Pereira, S. F., Goss, L., and Dworkin, J. (2011) Eukaryote-like serine/threonine kinases and phosphatases in bacteria. Microbiol. Mol. Biol. Rev. 75, 192-212
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 192-212
    • Pereira, S.F.1    Goss, L.2    Dworkin, J.3
  • 15
    • 0037969625 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis
    • DOI 10.1074/jbc.M300660200
    • Ortiz-Lombardía, M., Pompeo, F., Boitel, B., and Alzari, P. M. (2003) Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis. J. Biol. Chem. 278, 13094-13100 (Pubitemid 36800077)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 13094-13100
    • Ortiz-Lombardia, M.1    Pompeo, F.2    Boitel, B.3    Alzari, P.M.4
  • 16
    • 4444348265 scopus 로고    scopus 로고
    • Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases
    • LaRonde-LeBlanc, N., and Wlodawer, A. (2004) Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases. Structure 12, 1585-1594
    • (2004) Structure , vol.12 , pp. 1585-1594
    • LaRonde-LeBlanc, N.1    Wlodawer, A.2
  • 17
    • 22544465251 scopus 로고    scopus 로고
    • Structure and activity of the atypical serine kinase Rio1
    • DOI 10.1111/j.1742-4658.2005.04796.x
    • Laronde-Leblanc, N., Guszczynski, T., Copeland, T., and Wlodawer, A. (2005) Structure and activity of the atypical serine kinase Rio1. FEBS J. 272, 3698-3713 (Pubitemid 41021181)
    • (2005) FEBS Journal , vol.272 , Issue.14 , pp. 3698-3713
    • LaRonde-LeBlanc, N.1    Guszczynski, T.2    Copeland, T.3    Wlodawer, A.4
  • 18
    • 33846987910 scopus 로고    scopus 로고
    • Crystal structure of a novel prokaryotic Ser/Thr kinase and its implication in the Cpx stress response pathway
    • Zheng, J., He, C., Singh, V. K., Martin, N. L., and Jia, Z. (2007) Crystal structure of a novel prokaryotic Ser/Thr kinase and its implication in the Cpx stress response pathway. Mol. Microbiol. 63, 1360-1371
    • (2007) Mol. Microbiol. , vol.63 , pp. 1360-1371
    • Zheng, J.1    He, C.2    Singh, V.K.3    Martin, N.L.4    Jia, Z.5
  • 19
    • 0027511372 scopus 로고
    • ATP-dependent protein kinases in bacteria
    • Cozzone, A. J. (1993) ATP-dependent protein kinases in bacteria. J. Cell. Biochem. 51, 7-13
    • (1993) J. Cell. Biochem. , vol.51 , pp. 7-13
    • Cozzone, A.J.1
  • 20
    • 0029685972 scopus 로고    scopus 로고
    • The NTP phosphate donor in kinase reactions. Is ATP a monopolist?
    • Shugar, D. (1996) The NTP phosphate donor in kinase reactions. Is ATP a monopolist? Acta Biochim. Pol. 43, 9-23
    • (1996) Acta Biochim. Pol. , vol.43 , pp. 9-23
    • Shugar, D.1
  • 22
    • 70450255091 scopus 로고    scopus 로고
    • CaMKII uses GTP as a phosphate donor for both substrate and autophosphorylation
    • Bostrom, S. L., Dore, J., and Griffith, L. C. (2009) CaMKII uses GTP as a phosphate donor for both substrate and autophosphorylation. Biochem. Biophys. Res. Commun. 390, 1154-1159
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 1154-1159
    • Bostrom, S.L.1    Dore, J.2    Griffith, L.C.3
  • 23
    • 0030657770 scopus 로고    scopus 로고
    • Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements
    • DOI 10.1074/jbc.272.45.28695
    • Schinkmann, K., and Blenis, J. (1997) Cloning and characterization of a human STE20-like protein kinase with unusual cofactor requirements. J. Biol. Chem. 272, 28695-28703 (Pubitemid 27517826)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.45 , pp. 28695-28703
    • Schinkmann, K.1    Blenis, J.2
  • 25
    • 65449151891 scopus 로고    scopus 로고
    • Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2″-phosphotransferases
    • Toth, M., Chow, J. W., Mobashery, S., and Vakulenko, S. B. (2009) Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2″-phosphotransferases. J. Biol. Chem. 284, 6690-6696
    • (2009) J. Biol. Chem. , vol.284 , pp. 6690-6696
    • Toth, M.1    Chow, J.W.2    Mobashery, S.3    Vakulenko, S.B.4
  • 26
    • 77951231960 scopus 로고    scopus 로고
    • Nucleotide selectivity of antibiotic kinases
    • Shakya, T., and Wright, G. D. (2010) Nucleotide selectivity of antibiotic kinases. Antimicrob. Agents Chemother. 54, 1909-1913
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 1909-1913
    • Shakya, T.1    Wright, G.D.2
  • 27
    • 40449099074 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray analysis of aminoglycoside-2″-phosphotransferase-Ic [APH(2″)-Ic] from Enterococcus gallinarum
    • DOI 10.1107/S1744309108001450, PII S1744309108001450
    • Byrnes, L. J., Badarau, A., Vakulenko, S. B., and Smith, C. A. (2008) Purification, crystallization and preliminary X-ray analysis of aminoglycoside-2″-phosphotransferase-Ic [APH(2″)-Ic] from Enterococcus gallinarum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64, 126-129 (Pubitemid 351348078)
    • (2008) Acta Crystallographica Section F: Structural Biology and Crystallization Communications , vol.64 , Issue.2 , pp. 126-129
    • Byrnes, L.J.1    Badarau, A.2    Vakulenko, S.B.3    Smith, C.A.4
  • 28
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 29
    • 0242579382 scopus 로고    scopus 로고
    • A new class of lanthanide complexes to obtain high-phasing-power heavy-atom derivatives for macromolecular crystallography
    • DOI 10.1107/S0907444903020511
    • Girard, E., Stelter, M., Vicat, J., and Kahn, R. (2003) A new class of lanthanide complexes to obtain high-phasing-power heavy-atom derivatives for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 59, 1914-1922 (Pubitemid 37399324)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.11 , pp. 1914-1922
    • Girard, E.1    Stelter, M.2    Vicat, J.3    Kahn, R.4
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite. Programs for protein crystallography. Acta Crystallogr.DBiol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr.DBiol. Crystallogr. , vol.50 , pp. 760-763
  • 33
    • 0036784038 scopus 로고    scopus 로고
    • Mutations in the aph(2″)-Ic gene are responsible for increased levels of aminoglycoside resistance
    • Lee, H. K., Vakulenko, S. B., Clewell, D. B., Lerner, S. A., and Chow, J. W. (2002) Mutations in the aph(2″)-Ic gene are responsible for increased levels of aminoglycoside resistance. Antimicrob. Agents Chemother. 46, 3253-3256
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3253-3256
    • Lee, H.K.1    Vakulenko, S.B.2    Clewell, D.B.3    Lerner, S.A.4    Chow, J.W.5
  • 34
    • 67649413348 scopus 로고    scopus 로고
    • The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside- 2″-phosphotransferase-IIa [APH(2″)-IIa] provide insights into substrate selectivity in the APH(2″) subfamily
    • Young, P. G., Walanj, R., Lakshmi, V., Byrnes, L. J., Metcalf, P., Baker, E. N., Vakulenko, S. B., and Smith, C. A. (2009) The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside- 2″-phosphotransferase-IIa [APH(2″)-IIa] provide insights into substrate selectivity in the APH(2″) subfamily. J. Bacteriol. 191, 4133-4143
    • (2009) J. Bacteriol. , vol.191 , pp. 4133-4143
    • Young, P.G.1    Walanj, R.2    Lakshmi, V.3    Byrnes, L.J.4    Metcalf, P.5    Baker, E.N.6    Vakulenko, S.B.7    Smith, C.A.8
  • 35
    • 77955109419 scopus 로고    scopus 로고
    • Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase- 2″-IVa
    • Toth, M., Frase, H., Antunes, N. T., Smith, C. A., and Vakulenko, S. B. (2010) Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase- 2″-IVa. Protein Sci. 19, 1565-1576
    • (2010) Protein Sci. , vol.19 , pp. 1565-1576
    • Toth, M.1    Frase, H.2    Antunes, N.T.3    Smith, C.A.4    Vakulenko, S.B.5
  • 36
    • 0037459248 scopus 로고    scopus 로고
    • The crystal structure of aminoglycoside-3′-phospho-transferase-IIa, an enzyme responsible for antibiotic resistance
    • DOI 10.1016/S0022-2836(03)00121-9
    • Nurizzo, D., Shewry, S. C., Perlin, M. H., Brown, S. A., Dholakia, J. N., Fuchs, R. L., Deva, T., Baker, E. N., and Smith, C. A. (2003) The crystal structure of aminoglycoside-3′-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance. J. Mol. Biol. 327, 491-506 (Pubitemid 36298717)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.2 , pp. 491-506
    • Nurizzo, D.1    Shewry, S.C.2    Perlin, M.H.3    Brown, S.A.4    Dholakia, J.N.5    Fuchs, R.L.6    Deva, T.7    Baker, E.N.8    Smith, C.A.9
  • 37
    • 0030830868 scopus 로고    scopus 로고
    • Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases
    • Hon, W. C., McKay, G. A., Thompson, P. R., Sweet, R. M., Yang, D. S., Wright, G. D., and Berghuis, A. M. (1997) Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases. Cell 89, 887-895 (Pubitemid 27513515)
    • (1997) Cell , vol.89 , Issue.6 , pp. 887-895
    • Hon, W.-C.1    McKay, G.A.2    Thompson, P.R.3    Sweet, R.M.4    Yang, D.S.C.5    Wright, G.D.6    Berghuis, A.M.7
  • 38
  • 39
    • 77951225260 scopus 로고    scopus 로고
    • Structure of the antibiotic resistance factor spectinomycin phosphotransferase from Legionella pneumophila
    • Fong, D. H., Lemke, C. T., Hwang, J., Xiong, B., and Berghuis, A. M. (2010) Structure of the antibiotic resistance factor spectinomycin phosphotransferase from Legionella pneumophila. J. Biol. Chem. 285, 9545-9555
    • (2010) J. Biol. Chem. , vol.285 , pp. 9545-9555
    • Fong, D.H.1    Lemke, C.T.2    Hwang, J.3    Xiong, B.4    Berghuis, A.M.5
  • 40
    • 84860390496 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis Rv3168. A putative aminoglycoside antibiotics resistance enzyme
    • Kim, S., Nguyen, C. M., Kim, E. J., and Kim, K. J. (2011) Crystal structure of Mycobacterium tuberculosis Rv3168. A putative aminoglycoside antibiotics resistance enzyme. Proteins 79, 2983-2987
    • (2011) Proteins , vol.79 , pp. 2983-2987
    • Kim, S.1    Nguyen, C.M.2    Kim, E.J.3    Kim, K.J.4
  • 41
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • Zheng, J., Knighton, D. R., ten Eyck, L. F., Karlsson, R., Xuong, N., Taylor, S. S., and Sowadski, J. M. (1993) Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry 32, 2154-2161 (Pubitemid 23094874)
    • (1993) Biochemistry , vol.32 , Issue.9 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten, E.L.F.3    Karlsson, R.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 42
    • 0035979336 scopus 로고    scopus 로고
    • Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase
    • DOI 10.1021/bi010504p
    • Burk, D. L., Hon, W. C., Leung, A. K., and Berghuis, A. M. (2001) Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase. Biochemistry 40, 8756-8764 (Pubitemid 32709507)
    • (2001) Biochemistry , vol.40 , Issue.30 , pp. 8756-8764
    • Burk, D.L.1    Hon, W.C.2    Leung, A.K.-W.3    Berghuis, A.M.4
  • 43
    • 0034682564 scopus 로고    scopus 로고
    • Serine-53 at the tip of the glycine-rich loop of cAMP-dependent protein kinase. Role in catalysis, P-site specificity, and interaction with inhibitors
    • Aimes, R. T., Hemmer, W., and Taylor, S. S. (2000) Serine-53 at the tip of the glycine-rich loop of cAMP-dependent protein kinase. Role in catalysis, P-site specificity, and interaction with inhibitors. Biochemistry 39, 8325-8332
    • (2000) Biochemistry , vol.39 , pp. 8325-8332
    • Aimes, R.T.1    Hemmer, W.2    Taylor, S.S.3
  • 44
    • 79960255057 scopus 로고    scopus 로고
    • Crystal structures of antibiotic-bound complexes of aminoglycoside 2″-phosphotransferase IVa highlight the diversity in substrate binding modes among aminoglycoside kinases
    • Shi, K., Houston, D. R., and Berghuis, A. M. (2011) Crystal structures of antibiotic-bound complexes of aminoglycoside 2″-phosphotransferase IVa highlight the diversity in substrate binding modes among aminoglycoside kinases. Biochemistry 50, 6237-6244
    • (2011) Biochemistry , vol.50 , pp. 6237-6244
    • Shi, K.1    Houston, D.R.2    Berghuis, A.M.3
  • 45
    • 0036679979 scopus 로고    scopus 로고
    • A strategy for the design of multiplex inhibitors for kinase-mediated signalling in angiogenesis
    • DOI 10.1016/S1367-5931(02)00357-5
    • Adams, J., Huang, P., and Patrick, D. (2002) A strategy for the design of multiplex inhibitors for kinase-mediated signaling in angiogenesis. Curr. Opin. Chem. Biol. 6, 486-492 (Pubitemid 34804772)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.4 , pp. 486-492
    • Adams, J.1    Huang, P.2    Patrick, D.3
  • 47
    • 38149061122 scopus 로고    scopus 로고
    • Signaling through cAMP and cAMP-dependent protein kinase. Diverse strategies for drug design
    • Taylor, S. S., Kim, C., Cheng, C. Y., Brown, S. H., Wu, J., and Kannan, N. (2008) Signaling through cAMP and cAMP-dependent protein kinase. Diverse strategies for drug design. Biochim. Biophys. Acta 1784, 16-26
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 16-26
    • Taylor, S.S.1    Kim, C.2    Cheng, C.Y.3    Brown, S.H.4    Wu, J.5    Kannan, N.6
  • 48
    • 0033026444 scopus 로고    scopus 로고
    • Strategies toward the design of novel and selective protein tyrosine kinase inhibitors
    • DOI 10.1016/S0163-7258(98)00044-8, PII S0163725898000448
    • Traxler, P., and Furet, P. (1999) Strategies toward the design of novel and selective protein tyrosine kinase inhibitors. Pharmacol. Ther. 82, 195-206 (Pubitemid 29255915)
    • (1999) Pharmacology and Therapeutics , vol.82 , Issue.2-3 , pp. 195-206
    • Traxler, P.1    Furet, P.2
  • 49
    • 0011672458 scopus 로고    scopus 로고
    • ATP site-directed competitive and irreversible inhibitors of protein kinases
    • DOI 10.1002/(SICI)1098-1128(200001)20:1<28::AID-MED2>3.0.CO;2-2
    • García-Echeverría, C., Traxler, P., and Evans, D. B. (2000) ATP site-directed competitive and irreversible inhibitors of protein kinases. Med. Res. Rev. 20, 28-57 (Pubitemid 30027560)
    • (2000) Medicinal Research Reviews , vol.20 , Issue.1 , pp. 28-57
    • Garcia-Echeverria, C.1    Traxler, P.2    Evans, D.B.3
  • 50
    • 0035968312 scopus 로고    scopus 로고
    • Molecular mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa. Roles of conserved active site residues
    • Boehr, D. D., Thompson, P. R., and Wright, G. D. (2001) Molecular mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa. Roles of conserved active site residues. J. Biol. Chem. 276, 23929-23936
    • (2001) J. Biol. Chem. , vol.276 , pp. 23929-23936
    • Boehr, D.D.1    Thompson, P.R.2    Wright, G.D.3
  • 52
    • 67649726156 scopus 로고    scopus 로고
    • Protein kinase inhibitors. Contributions from structure to clinical compounds
    • Johnson, L. N. (2009) Protein kinase inhibitors. Contributions from structure to clinical compounds. Q. Rev. Biophys. 42, 1-40
    • (2009) Q. Rev. Biophys. , vol.42 , pp. 1-40
    • Johnson, L.N.1
  • 53
    • 24944521513 scopus 로고    scopus 로고
    • Establishing the principles of recognition in the adenine-binding region of an aminoglycoside antibiotic kinase [APH(3′)-IIIa]
    • DOI 10.1021/bi051085p
    • Boehr, D. D., Farley, A. R., LaRonde, F. J., Murdock, T. R., Wright, G. D., and Cox, J. R. (2005) Establishing the principles of recognition in the adenine binding region of an aminoglycoside antibiotic kinase [APH(3′)- IIIa]. Biochemistry 44, 12445-12453 (Pubitemid 41324336)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12445-12453
    • Boehr, D.D.1    Farley, A.R.2    LaRonde, F.J.3    Murdock, T.R.4    Wright, G.D.5    Cox, J.R.6
  • 54
    • 0037018922 scopus 로고    scopus 로고
    • Mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa. Role of the nucleotide positioning loop
    • Thompson, P. R., Boehr, D. D., Berghuis, A. M., and Wright, G. D. (2002) Mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa. Role of the nucleotide positioning loop. Biochemistry 41, 7001-7007
    • (2002) Biochemistry , vol.41 , pp. 7001-7007
    • Thompson, P.R.1    Boehr, D.D.2    Berghuis, A.M.3    Wright, G.D.4
  • 55
    • 0026717854 scopus 로고
    • Site-specific mutations of conserved C-terminal residues in aminoglycoside 3′-phosphotransferase II. Phenotypic and structural analysis of mutant enzymes
    • Kocabiyik, S., and Perlin, M. H. (1992) Site-specific mutations of conserved C-terminal residues in aminoglycoside 3′-phosphotransferase II. Phenotypic and structural analysis of mutant enzymes. Biochem. Biophys. Res. Commun. 185, 925-931
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 925-931
    • Kocabiyik, S.1    Perlin, M.H.2
  • 56
    • 0037093442 scopus 로고    scopus 로고
    • Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry
    • DOI 10.1093/emboj/21.10.2323
    • Fong, D. H., and Berghuis, A. M. (2002) Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry. EMBO J. 21, 2323-2331 (Pubitemid 34546705)
    • (2002) EMBO Journal , vol.21 , Issue.10 , pp. 2323-2331
    • Fong, D.H.1    Berghuis, A.M.2


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