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Volumn 19, Issue 4, 2010, Pages 763-774

An enriched structural kinase database to enable kinome-wide structure-based analyses and drug discovery

Author keywords

Binding sites; Catalytic domain; Crystallography: X ray; Databases: protein; Protein binding; Protein conformation; Protein kinases; Sequence analysis: protein; Structural informatics; Structure based drug design

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLYCINE; HELIX LOOP HELIX PROTEIN; PHOSPHOTRANSFERASE;

EID: 77950271944     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.355     Document Type: Article
Times cited : (47)

References (34)
  • 2
    • 3242884966 scopus 로고    scopus 로고
    • High-throughput docking as a source of novel drug leads
    • Alvarez JC (2004) High-throughput docking as a source of novel drug leads. Curr Opin Chem Biol 8:365-370.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 365-370
    • Alvarez, J.C.1
  • 3
    • 0030039619 scopus 로고    scopus 로고
    • The art and practice of structure-based drug design: A molecular modeling perspective
    • Bohacek RS, McMartin C, Guida WC (1996) The art and practice of structure-based drug design: a molecular modeling perspective. Med Res Rev 16:3-50.
    • (1996) Med Res Rev , vol.16 , pp. 3-50
    • Bohacek, R.S.1    McMartin, C.2    Guida, W.C.3
  • 4
    • 0348227698 scopus 로고    scopus 로고
    • The impact of structure-guided drug design on clinical agents
    • Hardy LW, Malikayil A (2003) The impact of structure-guided drug design on clinical agents. Curr Drug Discov December, 15-20.
    • (2003) Curr Drug Discov December , pp. 15-20
    • Hardy, L.W.1    Malikayil, A.2
  • 5
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • Hajduk PJ (2006) Fragment-based drug design: how big is too big? J Med Chem 49:6972-16697
    • (2006) J Med Chem , vol.49 , pp. 6972-16697
    • Hajduk, P.J.1
  • 7
    • 0036171255 scopus 로고    scopus 로고
    • SACS-self-maintaining database of antibody crystal structure information
    • Allcorn LC, Martin AC (2002) SACS-self-maintaining database of antibody crystal structure information. Bioinformatics 18:175-181.
    • (2002) Bioinformatics , vol.18 , pp. 175-181
    • Allcorn, L.C.1    Martin, A.C.2
  • 8
    • 39749162787 scopus 로고    scopus 로고
    • Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: Structure of lck/imatinib complex
    • Jacobs MD, Caron PR, Hare BJ (2008) Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of lck/imatinib complex. Proteins 70:1451-1460.
    • (2008) Proteins , vol.70 , pp. 1451-1460
    • Jacobs, M.D.1    Caron, P.R.2    Hare, B.J.3
  • 9
    • 0037436339 scopus 로고    scopus 로고
    • Relibase: Design and development of a database for comprehensive analysis of protein-ligand interactions
    • Hendlich M, Bergner A, Gunther J, Klebe G (2003) Relibase: design and development of a database for comprehensive analysis of protein-ligand interactions. J Mol Biol 326:607-620.
    • (2003) J Mol Biol , vol.326 , pp. 607-620
    • Hendlich, M.1    Bergner, A.2    Gunther, J.3    Klebe, G.4
  • 10
    • 0001731266 scopus 로고    scopus 로고
    • Use of Relibase for retrieving complex three-dimensional interaction patterns including crystallographic packing effects
    • Bergner A, Gunther J, Hendlich M, Klebe G, Verdonk M (2001) Use of Relibase for retrieving complex three-dimensional interaction patterns including crystallographic packing effects. Biopolymers 61:99-110.
    • (2001) Biopolymers , vol.61 , pp. 99-110
    • Bergner, A.1    Gunther, J.2    Hendlich, M.3    Klebe, G.4    Verdonk, M.5
  • 11
    • 58149092163 scopus 로고    scopus 로고
    • CREDO: A protein-ligand interaction database for drug discovery
    • Schreyer A, Blundell T (2009) CREDO: a protein-ligand interaction database for drug discovery. Chem Biol Drug Des 73:157-167.
    • (2009) Chem Biol Drug des , vol.73 , pp. 157-167
    • Schreyer, A.1    Blundell, T.2
  • 13
    • 33846108633 scopus 로고    scopus 로고
    • BindingDB: A web-accessible database of experimentally determined protein-ligand binding affinities
    • Liu T, Lin Y, Wen X, Jorissen RN, Gilson MK (2007) BindingDB: a web-accessible database of experimentally determined protein-ligand binding affinities. Nucleic Acids Res 35:D198-D201.
    • (2007) Nucleic Acids Res , vol.35
    • Liu, T.1    Lin, Y.2    Wen, X.3    Jorissen, R.N.4    Gilson, M.K.5
  • 14
  • 16
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-the major drug targets of the twenty-first century?
    • Cohen P (2002) Protein kinases-the major drug targets of the twenty-first century? Nat Rev Drug Discov 1: 309-315.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 309-315
    • Cohen, P.1
  • 17
    • 64349099558 scopus 로고    scopus 로고
    • Kinase domain mutations in cancer: Implications for small molecule drug design strategies
    • Bikker JA, Brooijmans N, Wissner A, Mansour TS (2009) Kinase domain mutations in cancer: implications for small molecule drug design strategies. J Med Chem 52:1493-1509.
    • (2009) J Med Chem , vol.52 , pp. 1493-1509
    • Bikker, J.A.1    Brooijmans, N.2    Wissner, A.3    Mansour, T.S.4
  • 19
    • 17644392830 scopus 로고    scopus 로고
    • TM-align: A protein structure alignment algorithm based on the TM-score
    • Zhang Y, Skolnick J (2005) TM-align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res 33:2302-2309.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2302-2309
    • Zhang, Y.1    Skolnick, J.2
  • 20
    • 0037436388 scopus 로고    scopus 로고
    • Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure
    • Akamine P, Madhusudan J, Xuong NH, Ten Eyck LF, Taylor SS (2003) Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure. J Mol Biol 327:159-171.
    • (2003) J Mol Biol , vol.327 , pp. 159-171
    • Akamine, P.1    Madhusudan, J.2    Xuong, N.H.3    Ten Eyck, L.F.4    Taylor, S.S.5
  • 21
    • 27644435575 scopus 로고    scopus 로고
    • Crystal structure of the E230Q mutant of cAMP-dependent protein kinase reveals an unexpected apoenzyme conformation and an extended N-terminal a helix
    • Wu J, Yang J, Kannan N, Madhusudan NH, Ten Eyck LF, Taylor SS (2005) Crystal structure of the E230Q mutant of cAMP-dependent protein kinase reveals an unexpected apoenzyme conformation and an extended N-terminal A helix. Protein Sci 14:2871-2879.
    • (2005) Protein Sci , vol.14 , pp. 2871-2879
    • Wu, J.1    Yang, J.2    Kannan, N.3    Madhusudan, N.H.4    Ten Eyck, L.F.5    Taylor, S.S.6
  • 22
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang J, Yang PL, Gray NS (2009) Targeting cancer with small molecule kinase inhibitors. Nat Rev Cancer 9:28-39.
    • (2009) Nat Rev Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 24
    • 0031226661 scopus 로고    scopus 로고
    • Database diversity assessment: New ideas, concepts, and tools
    • Nilakantan R, Bauman N, Haraki KS (1997) Database diversity assessment: new ideas, concepts, and tools. J Comput-Aided Mol Des 11:447-452.
    • (1997) J Comput-Aided Mol des , vol.11 , pp. 447-452
    • Nilakantan, R.1    Bauman, N.2    Haraki, K.S.3
  • 25
    • 77950220400 scopus 로고    scopus 로고
    • Available at
    • GVK. GVK Bio Databases. Available at: http://www.gvkbio.com/informatics. html August 2009.
    • GVK. GVK Bio Databases
  • 26
    • 53149132043 scopus 로고    scopus 로고
    • The development of HKI-272 and related compounds for the treatment of cancer
    • Wissner A, Mansour TS (2008) The development of HKI-272 and related compounds for the treatment of cancer. Arch Pharm 341:465-477.
    • (2008) Arch Pharm , vol.341 , pp. 465-477
    • Wissner, A.1    Mansour, T.S.2
  • 30
    • 23644452511 scopus 로고    scopus 로고
    • Did protein kinase regulatory mechanisms evolve through elaboration of a simple structural component?
    • Kannan N, Neuwald AF (2005) Did protein kinase regulatory mechanisms evolve through elaboration of a simple structural component? J Mol Biol 351:956-972.
    • (2005) J Mol Biol , vol.351 , pp. 956-972
    • Kannan, N.1    Neuwald, A.F.2
  • 31
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR (1998) Profile hidden Markov models. Bioinformatics 14:755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 32
    • 24944552075 scopus 로고    scopus 로고
    • High affinity targets of protein kinase inhibitors have similar residues at the positions energetically important for binding
    • DOI 10.1016/j.jmb.2005.07.074, PII S0022283605009009
    • Sheinerman FB, Giraud E, Laoui A (2005) High affinity targets of protein kinase inhibitors have similar residues at the positions energetically important for binding. J Mol Biol 352:1134-1156. (Pubitemid 41316721)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.5 , pp. 1134-1156
    • Sheinerman, F.B.1    Giraud, E.2    Laoui, A.3
  • 33
    • 77953324469 scopus 로고    scopus 로고
    • New York, NY: Schrodinger
    • Schrodinger (2007) Maestro 8.0. Manual. New York, NY: Schrodinger, p 294.
    • (2007) Maestro 8.0. Manual , pp. 294
    • Schrodinger1
  • 34
    • 77950201461 scopus 로고    scopus 로고
    • OpenEye Scientific Software
    • Santa Fe, NM: OpenEye Scientific Software, Inc.
    • OpenEye Scientific Software(2008) OEChemTK 1.6.0. Santa Fe, NM: OpenEye Scientific Software, Inc.
    • (2008) OEChemTK 1.6.0


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.