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Volumn 21, Issue 10, 2014, Pages 848-853

Energetic dissection of Gleevec's selectivity toward human tyrosine kinases

Author keywords

[No Author keywords available]

Indexed keywords

IMATINIB; PROTEIN TYROSINE KINASE; ABELSON KINASE; ANTINEOPLASTIC AGENT; BENZAMIDE DERIVATIVE; PIPERAZINE DERIVATIVE; PROTEIN BINDING; PROTEIN KINASE INHIBITOR; PYRIMIDINE DERIVATIVE;

EID: 84923367313     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2891     Document Type: Article
Times cited : (104)

References (35)
  • 1
    • 79953308071 scopus 로고    scopus 로고
    • Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms
    • Jura, N. et al. Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms. Mol. Cell 42, 9-22 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 9-22
    • Jura, N.1
  • 2
    • 75349091799 scopus 로고
    • Defining the conserved internal architecture of a protein kinase
    • Kornev, A.P., Taylor, S.S. Defining the conserved internal architecture of a protein kinase. Biochim. Biophys. Acta 1804, 440-444 (2010).
    • (1804) Biochim. Biophys. Acta , vol.440-444 , pp. 2010
    • Kornev, A.P.1    Taylor, S.S.2
  • 4
    • 63749113783 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: Thirty years and counting
    • Hunter, T. Tyrosine phosphorylation: thirty years and counting. Curr. Opin. Cell Biol. 21, 140-146 (2009).
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 140-146
    • Hunter, T.1
  • 5
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases: The major drug targets of the twenty-first century?
    • Cohen, P. Protein kinases: the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 1, 309-315 (2002).
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 309-315
    • Cohen, P.1
  • 6
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M., Kuriyan, J. The conformational plasticity of protein kinases. Cell 109, 275-282 (2002).
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 7
    • 34249818791 scopus 로고    scopus 로고
    • C-Abl tyrosine kinase and inhibition by the cancer drug imatinib (Gleevec/STI-571)
    • Nagar, B. c-Abl tyrosine kinase and inhibition by the cancer drug imatinib (Gleevec/STI-571). J. Nutr. 137, 1518S-1523S (2007).
    • (2007) J. Nutr , vol.137 , pp. 1518S-1523S
    • Nagar, B.1
  • 8
    • 0037459341 scopus 로고    scopus 로고
    • Variation on an Src-like theme
    • Harrison, S.C. Variation on an Src-like theme. Cell 112, 737-740 (2003).
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.C.1
  • 9
    • 33745164854 scopus 로고    scopus 로고
    • Activity of dual SRC-ABL inhibitors highlights the role of BCR/ABL kinase dynamics in drug resistance
    • Azam, M. et al. Activity of dual SRC-ABL inhibitors highlights the role of BCR/ABL kinase dynamics in drug resistance. Proc. Natl. Acad. Sci. USA 103, 9244-9249 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9244-9249
    • Azam, M.1
  • 10
    • 84867690864 scopus 로고    scopus 로고
    • Systems-pharmacology dissection of a drug synergy in imatinib-resistant CML
    • Winter, G.E. et al. Systems-pharmacology dissection of a drug synergy in imatinib-resistant CML. Nat. Chem. Biol. 8, 905-912 (2012).
    • (2012) Nat. Chem. Biol , vol.8 , pp. 905-912
    • Winter, G.E.1
  • 11
    • 79959476700 scopus 로고    scopus 로고
    • The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling
    • Dar, A.C., Shokat, K.M. The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling. Annu. Rev. Biochem. 80, 769-795 (2011).
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 769-795
    • Dar, A.C.1    Shokat, K.M.2
  • 12
    • 33847659183 scopus 로고    scopus 로고
    • C-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty
    • Seeliger, M.A. et al. c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty. Structure 15, 299-311 (2007).
    • (2007) Structure , vol.15 , pp. 299-311
    • Seeliger, M.A.1
  • 13
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • Nagar, B. et al. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). Cancer Res. 62, 4236-4243 (2002).
    • (2002) Cancer Res , vol.62 , pp. 4236-4243
    • Nagar, B.1
  • 14
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for STI-571 inhibition of abelson tyrosine kinase
    • Schindler, T. et al. Structural mechanism for STI-571 inhibition of abelson tyrosine kinase. Science 289, 1938-1942 (2000).
    • (2000) Science , vol.289 , pp. 1938-1942
    • Schindler, T.1
  • 15
    • 0031578579 scopus 로고    scopus 로고
    • The 2.35 A crystal structure of the inactivated form of chicken Src: A dynamic molecule with multiple regulatory interactions
    • Williams, J.C. et al. The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions. J. Mol. Biol. 274, 757-775 (1997).
    • (1997) J. Mol. Biol , vol.274 , pp. 757-775
    • Williams, J.C.1
  • 16
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu, W., Doshi, A., Lei, M., Eck, M.J., Harrison, S.C. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol. Cell 3, 629-638 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 17
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S.C., Eck, M.J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602 (1997).
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 18
    • 33646755174 scopus 로고    scopus 로고
    • A Src-like inactive conformation in the abl tyrosine kinase domain
    • Levinson, N.M. et al. A Src-like inactive conformation in the abl tyrosine kinase domain. PLoS Biol. 4, e144 (2006).
    • (2006) PLoS Biol , vol.4 , pp. e144
    • Levinson, N.M.1
  • 19
    • 77951557992 scopus 로고    scopus 로고
    • Molecular dynamics simulations show that conformational selection governs the binding preferences of imatinib for several tyrosine kinases
    • Aleksandrov, A., Simonson, T. Molecular dynamics simulations show that conformational selection governs the binding preferences of imatinib for several tyrosine kinases. J. Biol. Chem. 285, 13807-13815 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 13807-13815
    • Aleksandrov, A.1    Simonson, T.2
  • 20
    • 84873135773 scopus 로고    scopus 로고
    • Explaining why Gleevec is a specific and potent inhibitor of Abl kinase
    • Lin, Y.L., Meng, Y., Jiang, W., Roux, B. Explaining why Gleevec is a specific and potent inhibitor of Abl kinase. Proc. Natl. Acad. Sci. USA 110, 1664-1669 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1664-1669
    • Lin, Y.L.1    Meng, Y.2    Jiang, W.3    Roux, B.4
  • 21
    • 84856694630 scopus 로고    scopus 로고
    • The different flexibility of c-Src and c-Abl kinases regulates the accessibility of a druggable inactive conformation
    • Lovera, S. et al. The different flexibility of c-Src and c-Abl kinases regulates the accessibility of a druggable inactive conformation. J. Am. Chem. Soc. 134, 2496-2499 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 2496-2499
    • Lovera, S.1
  • 22
    • 20444399897 scopus 로고    scopus 로고
    • The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation
    • Cowan-Jacob, S.W. et al. The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation. Structure 13, 861-871 (2005).
    • (2005) Structure , vol.13 , pp. 861-871
    • Cowan-Jacob, S.W.1
  • 23
    • 53649083930 scopus 로고    scopus 로고
    • Small molecule recognition of c-Src via the Imatinib-binding conformation
    • Dar, A.C., Lopez, M.S., Shokat, K.M. Small molecule recognition of c-Src via the Imatinib-binding conformation. Chem. Biol. 15, 1015-1022 (2008).
    • (2008) Chem. Biol , vol.15 , pp. 1015-1022
    • Dar, A.C.1    Lopez, M.S.2    Shokat, K.M.3
  • 24
    • 49649108911 scopus 로고    scopus 로고
    • Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib
    • Vajpai, N. et al. Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. J. Biol. Chem. 283, 18292-18302 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 18292-18302
    • Vajpai, N.1
  • 25
    • 32044462537 scopus 로고    scopus 로고
    • NMR characterization of kinase p38 dynamics in free and ligand-bound forms
    • Vogtherr, M. et al. NMR characterization of kinase p38 dynamics in free and ligand-bound forms. Angew. Chem. Int. Edn. Engl. 45, 993-997 (2006).
    • (2006) Angew. Chem. Int. Edn. Engl , vol.45 , pp. 993-997
    • Vogtherr, M.1
  • 26
    • 58549114067 scopus 로고    scopus 로고
    • A conserved protonation-dependent switch controls drug binding in the Abl kinase
    • Shan, Y. et al. A conserved protonation-dependent switch controls drug binding in the Abl kinase. Proc. Natl. Acad. Sci. USA 106, 139-144 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 139-144
    • Shan, Y.1
  • 27
    • 84865166917 scopus 로고    scopus 로고
    • NMR line shapes and multi-state binding equilibria
    • Kovrigin, E.L. NMR line shapes and multi-state binding equilibria. J. Biomol. NMR 53, 257-270 (2012).
    • (2012) J. Biomol. NMR , vol.53 , pp. 257-270
    • Kovrigin, E.L.1
  • 28
    • 71549171706 scopus 로고    scopus 로고
    • Fitting enzyme kinetic data with KinTek Global Kinetic Explorer
    • Johnson, K.A. Fitting enzyme kinetic data with KinTek Global Kinetic Explorer. Methods Enzymol. 467, 601-626 (2009).
    • (2009) Methods Enzymol , vol.467 , pp. 601-626
    • Johnson, K.A.1
  • 29
    • 84855392245 scopus 로고    scopus 로고
    • Backbone assignment of the tyrosine kinase Src catalytic domain in complex with imatinib
    • Campos-Olivas, R., Marenchino, M., Scapozza, L., Gervasio, F.L. Backbone assignment of the tyrosine kinase Src catalytic domain in complex with imatinib. Biomol. NMR Assign. 5, 221-224 (2011).
    • (2011) Biomol. NMR Assign , vol.5 , pp. 221-224
    • Campos-Olivas, R.1    Marenchino, M.2    Scapozza, L.3    Gervasio, F.L.4
  • 30
    • 84888104464 scopus 로고    scopus 로고
    • NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors
    • Skora, L., Mestan, J., Fabbro, D., Jahnke, W., Grzesiek, S. NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors. Proc. Natl. Acad. Sci. USA 110, E4437-E4445 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. E4437-E4445
    • Skora, L.1    Mestan, J.2    Fabbro, D.3    Jahnke, W.4    Grzesiek, S.5
  • 31
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar, B. et al. Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 112, 859-871 (2003).
    • (2003) Cell , vol.112 , pp. 859-871
    • Nagar, B.1
  • 32
    • 60549112465 scopus 로고    scopus 로고
    • FitSpace explorer: An algorithm to evaluate multidimensional parameter space in fitting kinetic data
    • Johnson, K.A., Simpson, Z.B., Blom, T. FitSpace explorer: an algorithm to evaluate multidimensional parameter space in fitting kinetic data. Anal. Biochem. 387, 30-41 (2009).
    • (2009) Anal. Biochem , vol.387 , pp. 30-41
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 33
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson, U.B., Hallberg, B.M., Detitta, G.T., Dekker, N., Nordlund, P. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 357, 289-298 (2006).
    • (2006) Anal. Biochem , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 34
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 35
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: Development of a software pipeline
    • Vranken, W.F. et al. The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59, 687-696 (2005).
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1


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