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Volumn 50, Issue 43, 2011, Pages 9399-9408

Kinetic, mechanistic, and structural modeling studies of truncated wild-type leucine-rich repeat kinase 2 and the G2019S mutant

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; CATALYTIC MECHANISMS; CHEMICAL TRANSFER; CLOSED FORM; ENZYMATIC PROPERTIES; FRACTIONATION FACTORS; GENERAL BASE; GENETIC FACTORS; GTP BINDING; GTPASE ACTIVITY; HOMOLOGY MODELING; KINASE ACTIVITY; KINASE DOMAINS; KINETIC PROPERTIES; LEUCINE-RICH REPEATS; PARKINSONS DISEASE; PEPTIDE SUBSTRATES; SOLVENT KINETIC ISOTOPE EFFECTS; STRUCTURAL INTERPRETATION; STRUCTURAL MODELING; SUBSTRATE RECOGNITION; WILD TYPES;

EID: 80054979896     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201173d     Document Type: Article
Times cited : (42)

References (38)
  • 7
    • 33748993710 scopus 로고    scopus 로고
    • Kinase activity of mutant LRRK2 mediates neuronal toxicity
    • DOI 10.1038/nn1776, PII NN1776
    • Smith, W. W., Pei, Z., Jiang, H., Dawson, V. L., Dawson, T. M., and Ross, C. A. (2006) Kinase activity of mutant LRRK2 mediates neuronal toxicity Nat. Neurosci. 9, 1231-1233 (Pubitemid 44454261)
    • (2006) Nature Neuroscience , vol.9 , Issue.10 , pp. 1231-1233
    • Smith, W.W.1    Pei, Z.2    Jiang, H.3    Dawson, V.L.4    Dawson, T.M.5    Ross, C.A.6
  • 9
    • 34548604567 scopus 로고    scopus 로고
    • The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase thatstimulates kinase activity
    • DOI 10.1016/j.yexcr.2007.07.007, PII S0014482707003345
    • Guo, L., Gandhi, P. N., Wang, W., Petersen, R. B., Wilson-Delfosse, A. L., and Chen, S. G. (2007) The Parkinsons disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity Exp. Cell Res. 313, 3658-3670 (Pubitemid 47404550)
    • (2007) Experimental Cell Research , vol.313 , Issue.16 , pp. 3658-3670
    • Guo, L.1    Gandhi, P.N.2    Wang, W.3    Petersen, R.B.4    Wilson-Delfosse, A.L.5    Chen, S.G.6
  • 10
    • 33846818834 scopus 로고    scopus 로고
    • GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease
    • DOI 10.1021/bi061960m
    • Ito, G., Okai, T., Fujino, G., Takeda, K., Ichijo, H., Katada, T., and Iwatsubo, T. (2007) GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinsons disease Biochemistry 46, 1380-1388 (Pubitemid 46208485)
    • (2007) Biochemistry , vol.46 , Issue.5 , pp. 1380-1388
    • Ito, G.1    Okai, T.2    Fujino, G.3    Takeda, K.4    Ichijo, H.5    Katada, T.6    Iwatsubo, T.7
  • 16
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999) SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallogr. D55, 191-205 (Pubitemid 29053816)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 17
    • 0025398721 scopus 로고    scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Verind, G. (1996) WHAT IF: A molecular modeling and drug design program J. Mol. Graphics 8, 52-56
    • (1996) J. Mol. Graphics , vol.8 , pp. 52-56
    • Verind, G.1
  • 18
  • 20
    • 0020346954 scopus 로고
    • Solvent isotope effects of enzyme systems
    • Schowen, K. B. and Schowen, R. L. (1982) Solvent isotope effects of enzyme systems Methods Enzymol. 87, 551-606
    • (1982) Methods Enzymol. , vol.87 , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 22
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A New Approach for Rapid, Accurate Docking and Scoring. 2. Enrichment Factors in Database Screening
    • DOI 10.1021/jm030644s
    • Halgren, T. A., Murphy, R. B., Friesner, R. A., Beard, H. S., Frye, L. L., Pollard, W. T., and Banks, J. L. (2004) Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening J. Med. Chem. 47, 1750-1759 (Pubitemid 38380918)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.7 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6    Banks, J.L.7
  • 24
    • 23644452511 scopus 로고    scopus 로고
    • Did protein kinase regulatory mechanisms evolve through elaboration of a simple structural component?
    • DOI 10.1016/j.jmb.2005.06.057, PII S0022283605007266
    • Kannan, N. and Neuwald, A. F. (2005) Did protein kinase regulatory mechanisms evolve through elaboration of a simple structural component? J. Mol. Biol. 351, 956-972 (Pubitemid 41133444)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.5 , pp. 956-972
    • Kannan, N.1    Neuwald, A.F.2
  • 26
    • 55749102720 scopus 로고    scopus 로고
    • A helix scaffold for the assembly of active protein kinases
    • Kornev, A. P., Taylor, S. S., and Ten Eyck, L. F. (2008) A helix scaffold for the assembly of active protein kinases Proc. Natl. Acad. Sci. U.S.A. 105, 14377-14382
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14377-14382
    • Kornev, A.P.1    Taylor, S.S.2    Ten Eyck, L.F.3
  • 27
    • 0030859238 scopus 로고    scopus 로고
    • Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase
    • DOI 10.1074/jbc.272.27.16946
    • Hemmer, W., McGlone, M., Tsigelny, I., and Taylor, S. S. (1997) Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase J. Biol. Chem. 272, 16946-16954 (Pubitemid 27289797)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.27 , pp. 16946-16954
    • Hemmer, W.1    McGlone, M.2    Tsigelny, I.3    Taylor, S.S.4
  • 28
    • 70449377127 scopus 로고    scopus 로고
    • Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis
    • Parisiadou, L., Xie, C., Cho, H. J., Lin, X., Gu, X. L., Long, C. X., Lobbestael, E., Baekelandt, V., Taymans, J. M., Sun, L., and Cai, H. (2009) Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis J. Neurosci. 29, 13971-13980
    • (2009) J. Neurosci. , vol.29 , pp. 13971-13980
    • Parisiadou, L.1    Xie, C.2    Cho, H.J.3    Lin, X.4    Gu, X.L.5    Long, C.X.6    Lobbestael, E.7    Baekelandt, V.8    Taymans, J.M.9    Sun, L.10    Cai, H.11
  • 29
    • 68949218403 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 phosphorylates brain tubulin-β isoforms and modulates microtubule stability: A point of convergence in parkinsonian neurodegeneration?
    • Gillardon, F. (2009) Leucine-rich repeat kinase 2 phosphorylates brain tubulin-β isoforms and modulates microtubule stability: A point of convergence in parkinsonian neurodegeneration? J. Neurochem. 110, 1514-1522
    • (2009) J. Neurochem. , vol.110 , pp. 1514-1522
    • Gillardon, F.1
  • 30
    • 51949090816 scopus 로고    scopus 로고
    • Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila
    • Imai, Y., Gehrke, S., Wang, H. Q., Takahashi, R., Hasegawa, K., Oota, E., and Lu, B. (2008) Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila EMBO J. 27, 2432-2443
    • (2008) EMBO J. , vol.27 , pp. 2432-2443
    • Imai, Y.1    Gehrke, S.2    Wang, H.Q.3    Takahashi, R.4    Hasegawa, K.5    Oota, E.6    Lu, B.7
  • 31
    • 65649142038 scopus 로고    scopus 로고
    • The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro
    • Gloeckner, C. J., Schumacher, A., Boldt, K., and Ueffing, M. (2009) The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro J. Neurochem. 109, 959-968
    • (2009) J. Neurochem. , vol.109 , pp. 959-968
    • Gloeckner, C.J.1    Schumacher, A.2    Boldt, K.3    Ueffing, M.4
  • 35
    • 77749255337 scopus 로고    scopus 로고
    • Kinetic mechanistic studies of wild-type leucine-rich repeat kinase 2: Characterization of the kinase and GTPase activities
    • Liu, M., Dobson, B., Glicksman, M. A., Yue, Z., and Stein, R. L. (2010) Kinetic mechanistic studies of wild-type leucine-rich repeat kinase 2: Characterization of the kinase and GTPase activities Biochemistry 49, 2008-2017
    • (2010) Biochemistry , vol.49 , pp. 2008-2017
    • Liu, M.1    Dobson, B.2    Glicksman, M.A.3    Yue, Z.4    Stein, R.L.5
  • 37
    • 0026544171 scopus 로고
    • Low-barrier hydrogen bonds and low fractionation factor bases in enzymatic reactions
    • Cleland, W. W. (1992) Low-barrier hydrogen bonds and low fractionation factor bases in enzymatic reactions Biochemistry 31, 317-319
    • (1992) Biochemistry , vol.31 , pp. 317-319
    • Cleland, W.W.1
  • 38
    • 0025804778 scopus 로고
    • 2+-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-Å resolution
    • 2+-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-Å resolution Biochemistry 30, 2817-2822
    • (1991) Biochemistry , vol.30 , pp. 2817-2822
    • Lebioda, L.1    Stec, B.2


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