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Volumn 33, Issue 5, 2012, Pages 273-278

Structural approaches to obtain kinase selectivity

Author keywords

[No Author keywords available]

Indexed keywords

4 [[9 CHLORO 7 (2,6 DIFLUOROPHENYL) 5H PYRIMIDO[5,4 D][2]BENZAZEPIN 2 YL]AMINO]BENZOIC ACID; ADENOSINE TRIPHOSPHATE; ARQ 069; ARQ 523; AURORA A KINASE; CX 4945; CX 5011; CX 5279; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 8; DORAMAPIMOD; GLYCOGEN SYNTHASE KINASE 3BETA; IMATINIB; JWS 648; MYOSIN LIGHT CHAIN KINASE; P21 ACTIVATED KINASE 1; PD 318088; PD 334581; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PHOSPHOTRANSFERASE; PICTRELISIB; PONATINIB; PROTEIN KINASE INHIBITOR; PROTEIN KINASE PIM 1; S6 KINASE; SELUMETINIB; SORAFENIB; TIVANTINIB; UNCLASSIFIED DRUG; UNINDEXED DRUG; VASCULOTROPIN RECEPTOR 3;

EID: 84860524795     PISSN: 01656147     EISSN: 18733735     Source Type: Journal    
DOI: 10.1016/j.tips.2012.03.005     Document Type: Review
Times cited : (74)

References (47)
  • 2
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • DOI 10.1038/nchembio799, PII N799
    • Y. Liu, and N.S. Gray Rational design of inhibitors that bind to inactive kinase conformations Nat. Chem. Biol. 2 2006 358 364 (Pubitemid 43936934)
    • (2006) Nature Chemical Biology , vol.2 , Issue.7 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 4
    • 78650917050 scopus 로고    scopus 로고
    • Structural basis of CX-4945 binding to human protein kinase CK2
    • A.D. Ferguson Structural basis of CX-4945 binding to human protein kinase CK2 FEBS Lett. 585 2011 104 110
    • (2011) FEBS Lett. , vol.585 , pp. 104-110
    • Ferguson, A.D.1
  • 5
    • 80053397576 scopus 로고    scopus 로고
    • Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical trials for the treatment of cancer
    • R. Battistutta Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical trials for the treatment of cancer Biochemistry 50 2011 8478 8488
    • (2011) Biochemistry , vol.50 , pp. 8478-8488
    • Battistutta, R.1
  • 6
    • 84857380650 scopus 로고    scopus 로고
    • Rational approaches to improving selectivity in drug design
    • D.J. Huggins Rational approaches to improving selectivity in drug design J. Med. Chem. 55 2012 1424 1444
    • (2012) J. Med. Chem. , vol.55 , pp. 1424-1444
    • Huggins, D.J.1
  • 7
    • 77950678935 scopus 로고    scopus 로고
    • Understanding kinase selectivity through energetic analysis of binding site waters
    • D.D. Robinson Understanding kinase selectivity through energetic analysis of binding site waters Chem. Med. Chem. 5 2010 618 627
    • (2010) Chem. Med. Chem. , vol.5 , pp. 618-627
    • Robinson, D.D.1
  • 8
    • 80054736907 scopus 로고    scopus 로고
    • Structural basis for activation and inhibition of class i phosphoinositide 3-kinases
    • O. Vadas Structural basis for activation and inhibition of class I phosphoinositide 3-kinases Sci. Signaling 4 2011 1 12
    • (2011) Sci. Signaling , vol.4 , pp. 1-12
    • Vadas, O.1
  • 9
    • 75349106113 scopus 로고    scopus 로고
    • The p110δ structure: Mechanisms for selectivity and potency of new PI(3)K inhibitors
    • A. Berndt The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors Nat. Chem. Biol. 6 2010 117 124
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 117-124
    • Berndt, A.1
  • 10
    • 81555223852 scopus 로고    scopus 로고
    • Rational design of phosphoinositide 3-kinase α inhibitors that exhibit selectivity over the phosphoinositide 3-kinase β isoform
    • T. Heffron Rational design of phosphoinositide 3-kinase α inhibitors that exhibit selectivity over the phosphoinositide 3-kinase β isoform J. Med. Chem. 54 2011 7815 7833
    • (2011) J. Med. Chem. , vol.54 , pp. 7815-7833
    • Heffron, T.1
  • 11
    • 77950473958 scopus 로고    scopus 로고
    • Kinase selectivity potential for inhibitors targeting the ATP binding site: A network analysis
    • D. Huang Kinase selectivity potential for inhibitors targeting the ATP binding site: a network analysis Bioinformatics 26 2010 198 204
    • (2010) Bioinformatics , vol.26 , pp. 198-204
    • Huang, D.1
  • 12
    • 80052015102 scopus 로고    scopus 로고
    • Profile-QSAR: A novel meta-QSAR method that combines activities across the kinase family to accurately predict affinity, selectivity, and cellular activity
    • E. Martin Profile-QSAR: a novel meta-QSAR method that combines activities across the kinase family to accurately predict affinity, selectivity, and cellular activity J. Chem. Inf. Model. 51 2011 1942 1956
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 1942-1956
    • Martin, E.1
  • 13
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • S.S. Taylor, and A.P. Kornev Protein kinases: evolution of dynamic regulatory proteins Trends Biochem. Sci. 36 2011 65 77
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 14
    • 77953458271 scopus 로고    scopus 로고
    • ARQ 197, a novel and selective inhibitor of the human c-Met receptor tyrosine kinase with antitumor activity
    • N. Munshi ARQ 197, a novel and selective inhibitor of the human c-Met receptor tyrosine kinase with antitumor activity Mol. Cancer Ther. 9 2010 1544 1553
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 1544-1553
    • Munshi, N.1
  • 15
    • 79957985551 scopus 로고    scopus 로고
    • Discovery of a novel mode of protein kinase inhibition characterised by the mechanism of inhibition of human mesenchymal-epithelial transition factor (c-Met) protein autophosphorylation by ARQ 197
    • S. Eathiraj Discovery of a novel mode of protein kinase inhibition characterised by the mechanism of inhibition of human mesenchymal-epithelial transition factor (c-Met) protein autophosphorylation by ARQ 197 J. Biol. Chem. 286 2011 20666 20676
    • (2011) J. Biol. Chem. , vol.286 , pp. 20666-20676
    • Eathiraj, S.1
  • 16
    • 79958002291 scopus 로고    scopus 로고
    • A novel mode of protein kinase inhibition exploiting hydrophobic motifs of auto-inhibited kinases: Discovery of ATP independent inhibitors of fibroblast growth factor receptor (FGFR)
    • S. Eathiraj A novel mode of protein kinase inhibition exploiting hydrophobic motifs of auto-inhibited kinases: discovery of ATP independent inhibitors of fibroblast growth factor receptor (FGFR) J. Biol. Chem. 286 2011 20677 20687
    • (2011) J. Biol. Chem. , vol.286 , pp. 20677-20687
    • Eathiraj, S.1
  • 17
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase
    • T. Schindler Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase Science 289 2000 1938 1942
    • (2000) Science , vol.289 , pp. 1938-1942
    • Schindler, T.1
  • 18
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • DOI 10.1038/nchembio799, PII N799
    • N.S. Gray Rational design of inhibitors that bind to inactive kinase conformations Nat Chem. Biol. 2 2006 358 364 (Pubitemid 43936934)
    • (2006) Nature Chemical Biology , vol.2 , Issue.7 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 19
    • 77955413396 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of 8 hybrid DFG-out allosteric kinase inhibitors: A structural analysis of the binding interactions of Gleevec, Nexavar, and BIRB-796
    • J. Dietrich The design, synthesis, and evaluation of 8 hybrid DFG-out allosteric kinase inhibitors: a structural analysis of the binding interactions of Gleevec, Nexavar, and BIRB-796 Bioorg. Med. Chem. 18 2010 5738 5748
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 5738-5748
    • Dietrich, J.1
  • 20
    • 77951689893 scopus 로고    scopus 로고
    • Analysis of imatinib and sorafenib binding to p38α compared with c-Abl and b-Raf provides structural insights for the understanding the selectivity of inhibitors targeting the DFG-out form of protein kinases
    • H.V. Namboodiri Analysis of imatinib and sorafenib binding to p38α compared with c-Abl and b-Raf provides structural insights for the understanding the selectivity of inhibitors targeting the DFG-out form of protein kinases Biochemistry 49 2010 3611 3618
    • (2010) Biochemistry , vol.49 , pp. 3611-3618
    • Namboodiri, H.V.1
  • 21
    • 58149102648 scopus 로고    scopus 로고
    • Type-II kinase inhibitor docking, screening, and profiling using modified structures of active kinase states
    • I. Kufareva, and R. Abagyan Type-II kinase inhibitor docking, screening, and profiling using modified structures of active kinase states J. Med. Chem. 51 2008 7921 7932
    • (2008) J. Med. Chem. , vol.51 , pp. 7921-7932
    • Kufareva, I.1    Abagyan, R.2
  • 22
    • 79960817172 scopus 로고    scopus 로고
    • Predicting inactive conformations of protein kinases using active structures: Conformational selection of Type-II inhibitors
    • M. Xu Predicting inactive conformations of protein kinases using active structures: conformational selection of Type-II inhibitors PLoS ONE 6 2011 e22644
    • (2011) PLoS ONE , vol.6 , pp. 22644
    • Xu, M.1
  • 23
    • 79957497448 scopus 로고    scopus 로고
    • Discovery of a potential allosteric ligand binding site in CDK2
    • S. Betzi Discovery of a potential allosteric ligand binding site in CDK2 ACS Chem. Biol. 6 2011 492 501
    • (2011) ACS Chem. Biol. , vol.6 , pp. 492-501
    • Betzi, S.1
  • 24
    • 80052034056 scopus 로고    scopus 로고
    • The structure of CDK8/CycC implicates specificity in the CDK/Cyclin family and reveals interaction with a deep pocket binder
    • E.V. Schneider The structure of CDK8/CycC implicates specificity in the CDK/Cyclin family and reveals interaction with a deep pocket binder J. Mol. Biol. 412 2011 251 266
    • (2011) J. Mol. Biol. , vol.412 , pp. 251-266
    • Schneider, E.V.1
  • 25
    • 15744380263 scopus 로고    scopus 로고
    • Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition
    • J.F. Ohren Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition Nat. Struct. Mol. Biol. 11 2004 1192 1197
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1192-1197
    • Ohren, J.F.1
  • 27
    • 57749119314 scopus 로고    scopus 로고
    • Beyond the MEK-pocket: Can current MEK kinase inhibitors be utilized to synthesize novel type III NCKIs? Does the MEK-pocket exist in kinases other than MEK?
    • H. Tecle Beyond the MEK-pocket: can current MEK kinase inhibitors be utilized to synthesize novel type III NCKIs? Does the MEK-pocket exist in kinases other than MEK? Bioorg. Med. Chem. Lett. 19 2009 226 269
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 226-269
    • Tecle, H.1
  • 28
    • 64349099558 scopus 로고    scopus 로고
    • Kinase domain mutations in cancer: Implications for small molecule drug design strategies
    • J.A. Bikker Kinase domain mutations in cancer: implications for small molecule drug design strategies J. Med. Chem. 52 2009 1493 1509
    • (2009) J. Med. Chem. , vol.52 , pp. 1493-1509
    • Bikker, J.A.1
  • 29
    • 75749146285 scopus 로고    scopus 로고
    • Biochemical mechanisms of resistance to small-molecule protein kinase inhibitors
    • D.J. Maly Biochemical mechanisms of resistance to small-molecule protein kinase inhibitors ACS Chem. Biol. 5 2010 121 138
    • (2010) ACS Chem. Biol. , vol.5 , pp. 121-138
    • Maly, D.J.1
  • 30
    • 77950878509 scopus 로고    scopus 로고
    • Crystal structure of an Aurora-A mutant that mimics Aurora-B bound to MLN8054: Insights into selectivity and drug design
    • C.A. Dodson Crystal structure of an Aurora-A mutant that mimics Aurora-B bound to MLN8054: insights into selectivity and drug design Biochem. J. 427 2010 19 28
    • (2010) Biochem. J. , vol.427 , pp. 19-28
    • Dodson, C.A.1
  • 31
    • 79957958724 scopus 로고    scopus 로고
    • Recent developments in the third generation inhibitors of Bcr-Abl for overriding T315I mutation
    • X.Y. Lu Recent developments in the third generation inhibitors of Bcr-Abl for overriding T315I mutation Curr. Med. Chem. 18 2011 2146 2157
    • (2011) Curr. Med. Chem. , vol.18 , pp. 2146-2157
    • Lu, X.Y.1
  • 32
    • 70350507997 scopus 로고    scopus 로고
    • AP24534, a Pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance
    • T. O'Hare AP24534, a Pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance Cancer Cell 16 2009 401 412
    • (2009) Cancer Cell , vol.16 , pp. 401-412
    • O'Hare, T.1
  • 33
    • 78650159009 scopus 로고    scopus 로고
    • Structural mechanism of the pan-BCR-ABL inhibitor ponatinib (AP24534): Lessons for overcoming kinase inhibitor resistance
    • T. Zhou Structural mechanism of the pan-BCR-ABL inhibitor ponatinib (AP24534): lessons for overcoming kinase inhibitor resistance Chem. Biol. Drug Des. 77 2011 1 11
    • (2011) Chem. Biol. Drug Des. , vol.77 , pp. 1-11
    • Zhou, T.1
  • 34
    • 0030893008 scopus 로고    scopus 로고
    • Structure-based design of a potent, selective, and irreversible inhibitor of the catalytic domain of the erbB receptor subfamily of protein tyrosine kinases
    • DOI 10.1021/jm960380s
    • J. Singh Structure-based design of a potent, selective, and irreversible inhibitor of the catalytic domain of the ErbB receptor subfamily of protein tyrosine kinases J. Med. Chem. 40 1997 1130 1135 (Pubitemid 27149266)
    • (1997) Journal of Medicinal Chemistry , vol.40 , Issue.7 , pp. 1130-1135
    • Singh, J.1    Dobrusin, E.M.2    Fry, D.W.3    Haske, T.4    Whitty, A.5    McNamara, D.J.6
  • 35
    • 79953314480 scopus 로고    scopus 로고
    • The resurgence of covalent drugs
    • J. Singh The resurgence of covalent drugs Nat. Rev. Drug Discov. 10 2011 307 317
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 307-317
    • Singh, J.1
  • 36
    • 19744364796 scopus 로고    scopus 로고
    • Biochemistry: Structural bioinformatics-based design of selective, irreversible kinase inhibitors
    • DOI 10.1126/science1108367
    • M.S. Cohen Structural bioinformatics-based design of selective, irreversible kinase inhibitors Science 308 2005 1318 1321 (Pubitemid 40746129)
    • (2005) Science , vol.308 , Issue.5726 , pp. 1318-1321
    • Cohen, M.S.1    Zhang, C.2    Shokat, K.M.3    Taunton, J.4
  • 37
    • 77955982439 scopus 로고    scopus 로고
    • Structural biology in fragment-based drug design
    • C.W. Murray, and T.L. Blundell Structural biology in fragment-based drug design Curr. Opin. Struct. Biol. 20 2010 497 507
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 497-507
    • Murray, C.W.1    Blundell, T.L.2
  • 38
    • 65349195698 scopus 로고    scopus 로고
    • Molecular docking and ligand specificity in fragment-based inhibitor discovery
    • Y. Chen, and B.K. Shoichet Molecular docking and ligand specificity in fragment-based inhibitor discovery Nat. Chem. Biol. 5 2009 358 364
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 358-364
    • Chen, Y.1    Shoichet, B.K.2
  • 39
    • 77954724107 scopus 로고    scopus 로고
    • Ligand specificity in fragment-based drug design
    • S. Barelier Ligand specificity in fragment-based drug design J. Med. Chem. 53 2010 5256 5266
    • (2010) J. Med. Chem. , vol.53 , pp. 5256-5266
    • Barelier, S.1
  • 40
    • 79960637446 scopus 로고    scopus 로고
    • Selectivity of kinase inhibitor fragments
    • P. Bamborough Selectivity of kinase inhibitor fragments J. Med. Chem. 54 2011 5131 5143
    • (2011) J. Med. Chem. , vol.54 , pp. 5131-5143
    • Bamborough, P.1
  • 41
    • 79955556517 scopus 로고    scopus 로고
    • Discovery of a potent and highly selective PDK1 inhibitor via fragment-based drug discovery
    • D.A. Erlanson Discovery of a potent and highly selective PDK1 inhibitor via fragment-based drug discovery Bioorg. Med. Chem. Lett. 21 2011 3078 3083
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 3078-3083
    • Erlanson, D.A.1
  • 42
    • 79954541159 scopus 로고    scopus 로고
    • Structurally sophisticated octahedral metal complexes as highly selective protein kinase inhibitors
    • L. Feng Structurally sophisticated octahedral metal complexes as highly selective protein kinase inhibitors J. Am. Chem. Soc. 133 2011 5976 5986
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5976-5986
    • Feng, L.1
  • 43
    • 84855973740 scopus 로고    scopus 로고
    • Dual anticancer activity in a single compound: Visible-light-induced apoptosis by an antiangiogenic iridium complex
    • A. Kastl Dual anticancer activity in a single compound: visible-light-induced apoptosis by an antiangiogenic iridium complex Chem. Commun. 48 2012 1863 1865
    • (2012) Chem. Commun. , vol.48 , pp. 1863-1865
    • Kastl, A.1
  • 44
    • 78650657590 scopus 로고    scopus 로고
    • Tinkering outside the kinase ATP box: Allosteric (type IV) and bivalent (type V) inhibitors of protein kinases
    • K.J. Cox Tinkering outside the kinase ATP box: allosteric (type IV) and bivalent (type V) inhibitors of protein kinases Future Med. Chem. 3 2011 29 43
    • (2011) Future Med. Chem. , vol.3 , pp. 29-43
    • Cox, K.J.1
  • 45
    • 0033178359 scopus 로고    scopus 로고
    • The development and therapeutic potential of protein kinase inhibitors
    • DOI 10.1016/S1367-5931(99)80067-2
    • P. Cohen The development and therapeutic potential of protein kinase inhibitors Curr. Opin. Chem. Biol. 3 1999 459 465 (Pubitemid 29376108)
    • (1999) Current Opinion in Chemical Biology , vol.3 , Issue.4 , pp. 459-465
    • Cohen, P.1
  • 46
    • 77649204688 scopus 로고    scopus 로고
    • Selectively nonselective kinase inhibition: Striking the right balance
    • R. Morphy Selectively nonselective kinase inhibition: striking the right balance J. Med. Chem. 53 2010 1413 1437
    • (2010) J. Med. Chem. , vol.53 , pp. 1413-1437
    • Morphy, R.1
  • 47
    • 80255131239 scopus 로고    scopus 로고
    • Kinetic efficiency: The missing metric for enhancing compound quality?
    • G.A. Holdgate, and A.L. Gill Kinetic efficiency: the missing metric for enhancing compound quality? Drug Discov. Today 16 2011 910 913
    • (2011) Drug Discov. Today , vol.16 , pp. 910-913
    • Holdgate, G.A.1    Gill, A.L.2


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