메뉴 건너뛰기




Volumn 75, Issue 3, 2009, Pages 671-681

Structural basis for the complete loss of GSK3β catalytic activity due to R96 mutation investigated by molecular dynamics study

Author keywords

Electronic interaction; Glycogen synthesis kinase 3; MM GBSA; Molecular dynamics simulation; Phospho ser

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININE; GLYCOGEN SYNTHASE KINASE 3BETA; PHOSPHATE; PHOSPHOSERINE;

EID: 66149130737     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22279     Document Type: Article
Times cited : (16)

References (75)
  • 2
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation - A 25-year update
    • Cohen P. The regulation of protein function by multisite phosphorylation - a 25-year update. Trends Biochem Sci 2000;25:596-601.
    • (2000) Trends Biochem Sci , vol.25 , pp. 596-601
    • Cohen, P.1
  • 3
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter T. Signaling-2000 and beyond. Cell 2000;100:113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 4
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • DOI 10.1016/S0092-8674(00)81092-2
    • Johnson LN, Noble MEM, Owen DJ. Active and inactive protein kinases: structural basis for regulation. Cell 1996;85:149-158. (Pubitemid 26118158)
    • (1996) Cell , vol.85 , Issue.2 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 5
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • DOI 10.1021/cr000225s
    • Johnson LN, Lewis RJ. Structural basis for control by phosphorylation. Chem Rev 2001;101:2209-2242. (Pubitemid 35373017)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 6
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • DOI 10.1016/j.molcel.2004.08.024, PII S1097276504004800
    • Nolen B, Taylor S, Ghosh G. Regulation of protein kinases: controlling activity through activation segment conformation. Mol Cell 2004;15:661-675. (Pubitemid 39194898)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 7
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • DOI 10.1016/S0092-8674(02)00741-9
    • Huse M, John K. The conformational plasticity of protein kinases. Cell 2002;109:275-282. (Pubitemid 34606870)
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 8
    • 0025739664 scopus 로고
    • Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions
    • Gibbs CS, Zoller MJ. Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions. J Biol Chem 1991;266:8923-8931. (Pubitemid 21906599)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.14 , pp. 8923-8931
    • Gibbs, C.S.1    Zoller, M.J.2
  • 9
    • 0035964253 scopus 로고    scopus 로고
    • Electrostatic environment surrounding the activation loop phosphotyrosine in the oncoprotein v-Fps
    • DOI 10.1021/bi010838e
    • Leon BC, Tsigelny I, Adams JA. Electrostatic environment surrounding the activation loop phosphotyrosine in the oncoprotein v-Fps. Biochemistry 2001;40:10078-10086. (Pubitemid 32800115)
    • (2001) Biochemistry , vol.40 , Issue.34 , pp. 10078-10086
    • Chie Leon, B.1    Tsigelny, I.2    Adams, J.A.3
  • 12
    • 34250166523 scopus 로고    scopus 로고
    • Evolved to Be Active: Sulfate Ions Define Substrate Recognition Sites of CK2α and Emphasise its Exceptional Role within the CMGC Family of Eukaryotic Protein Kinases
    • DOI 10.1016/j.jmb.2007.04.068, PII S0022283607005815
    • Niefind K, Yde CW, Ermakova I, Issinger O-G. Evolved to be active: sulfate ions define substrate recognition sites of CK2α and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases. J Mol Biol 2007;370:427-438. (Pubitemid 46898435)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.3 , pp. 427-438
    • Niefind, K.1    Yde, C.W.2    Ermakova, I.3    Issinger, O.-G.4
  • 13
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/Factor a
    • Woodgett JR. Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J 1990;9:2431-2438. (Pubitemid 20218338)
    • (1990) EMBO Journal , vol.9 , Issue.8 , pp. 2431-2438
    • Woodgett, J.R.1
  • 14
    • 0035413614 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3: Properties, functions, and regulation
    • DOI 10.1021/cr000110o
    • Ali A, Hoeflich KP, Woodgett JR. Glycogen synthase kinase-3: properties, functions, and regulation. Chem Rev 2001;10:2527-2540. (Pubitemid 35373033)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2527-2540
    • Ali, A.1    Hoeflich, K.P.2    Woodgett, J.R.3
  • 16
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • DOI 10.1242/jcs.00384
    • Doble BW, Woodgett JR. GSK-3: tricks of the trade for a multitasking kinase. J Cell Sci 2003;116:1175-1186. (Pubitemid 36410657)
    • (2003) Journal of Cell Science , vol.116 , Issue.7 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 17
    • 0036090823 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3: An emerging therapeutic target
    • Hagit EF. Glycogen synthase kinase-3: an emerging therapeutic target. Trends Mol Med 2002;8:8126-8132.
    • (2002) Trends Mol Med , vol.8 , pp. 8126-8132
    • Hagit, E.F.1
  • 18
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • DOI 10.1042/0264-6021:3590001
    • Fram S, Cohen P. GSK3 takes center stage more than 20 years after its discovery. Biochem J 2001;359:1-16. (Pubitemid 32939202)
    • (2001) Biochemical Journal , vol.359 , Issue.1 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 19
    • 0442276554 scopus 로고    scopus 로고
    • The glamour and gloom of glycogen synthase kinase-3
    • DOI 10.1016/j.tibs.2003.12.004
    • Jope RS, Johnson GV. The glamour and gloom of glycogen synthase kinase-3. Trends Biochem Sci 2004;26:95-102. (Pubitemid 38186580)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.2 , pp. 95-102
    • Jope, R.S.1    Johnson, G.V.W.2
  • 20
    • 1642286981 scopus 로고    scopus 로고
    • GSK-3 inhibitors: Discoveries and developments
    • DOI 10.2174/0929867043455738
    • Alonso M, Martinez A. GSK-3 inhibitors: discoveries and developments. Curr Med Chem 2004;11:755-763. (Pubitemid 38380049)
    • (2004) Current Medicinal Chemistry , vol.11 , Issue.6 , pp. 755-763
    • Alonso, M.1    Martinez, A.2
  • 21
    • 34249861511 scopus 로고    scopus 로고
    • Identification of potential glycogen kinase-3 inhibitors by structure based virtual screening
    • DOI 10.1016/j.bpc.2007.04.001, PII S030146220700083X
    • Dessalew N, Bharatam PV. Identification of potential glycogen kinase-3 inhibitors by structure based virtual screening. Biophys Chem 2007;128:165-175. (Pubitemid 46860305)
    • (2007) Biophysical Chemistry , vol.128 , Issue.2-3 , pp. 165-175
    • Dessalew, N.1    Bharatam, P.V.2
  • 23
    • 0032821768 scopus 로고    scopus 로고
    • A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of Axin and β-catenin
    • DOI 10.1016/S0014-5793(99)01161-8, PII S0014579399011618
    • Thomas GMA. GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of axin and L-catenin. FEBS Lett 1999;458:247-251. (Pubitemid 29428192)
    • (1999) FEBS Letters , vol.458 , Issue.2 , pp. 247-251
    • Thomas, G.M.1    Frame, S.2    Goedert, M.3    Nathke, I.4    Polakis, P.5    Cohen, P.6
  • 24
    • 0023656594 scopus 로고
    • Formation of protein kinase recognition sites by covalent modification of the substrate, molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3
    • Fiol CJ, Mahrenholz AM, Wang Y, Roeske RW, Roach PJ. Formation of protein kinase recognition sites by covalent modification of the substrate, molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3. J Biol Chem 1987;262:14042-14048.
    • (1987) J Biol Chem , vol.262 , pp. 14042-14048
    • Fiol, C.J.1    Mahrenholz, A.M.2    Wang, Y.3    Roeske, R.W.4    Roach, P.J.5
  • 25
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • Welsh GI, Proud CG. Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem J 1993;294:625-629. (Pubitemid 23286543)
    • (1993) Biochemical Journal , vol.294 , Issue.3 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 26
    • 0032498112 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
    • DOI 10.1016/S0014-5793(97)01548-2, PII S0014579397015482
    • Welsh GI, Miller CM, Loughlin AJ, Price NT, Proud CG. Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett 1998;421:125-130. (Pubitemid 28288076)
    • (1998) FEBS Letters , vol.421 , Issue.2 , pp. 125-130
    • Welsh, G.I.1    Miller, C.M.2    Loughlin, A.J.3    Price, N.T.4    Proud, C.G.5
  • 27
    • 0029683606 scopus 로고    scopus 로고
    • The axis-inducing activity, stability, and subcellular distribution of β-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3
    • Yost C, Torres M, Miller JR, Huang E, Kimerlman D, Moon RT. The axis-inducing activity, stability, and subcellular distribution of beta-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3. Genes Dev 1996;10:1443-1454. (Pubitemid 26260702)
    • (1996) Genes and Development , vol.10 , Issue.12 , pp. 1443-1454
    • Yost, C.1    Torres, M.2    Miller, J.R.3    Huang, E.4    Kimelman, D.5    Moon, R.T.6
  • 28
    • 0141593670 scopus 로고    scopus 로고
    • Phosphorylation of β-catenin at S33, S37 or T41 can occur in the absence of phosphorylation of T45 in colon cancer cells
    • Wang Z, Vogelstein B, Kinzler KW. Phosphorylation of β-catenin at S33, S37 or T41 can occur in the absence of phosphorylation of T45 in colon cancer cells. Cancer Res 2003;63:5234-5235.
    • (2003) Cancer Res , vol.63 , pp. 5234-5235
    • Wang, Z.1    Vogelstein, B.2    Kinzler, K.W.3
  • 29
    • 0037415737 scopus 로고    scopus 로고
    • Structural basis for recruitment of glycogen synthase kinase 3β to the axin-APC scaffold complex
    • DOI 10.1093/emboj/cdg068
    • Dajani R, Fraser E, Roe SM, Yeo M, Good VM, Thompson V, Dale TC, Pear LH. Structural basis for recruitment of glycogen synthase kinase 3b to the axin-APC scaffold complex. EMBO J 2003;22:494-501. (Pubitemid 36193594)
    • (2003) EMBO Journal , vol.22 , Issue.3 , pp. 494-501
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Yeo, M.4    Good, V.M.5    Thompson, V.6    Dale, T.C.7    Pearl, L.H.8
  • 30
    • 0037155691 scopus 로고    scopus 로고
    • Control of β-catenin phosphorylation/degradation by a dual-kinase mechanism
    • DOI 10.1016/S0092-8674(02)00685-2
    • Liu C, Li Y, Semenov M, Han C, Baeg GH, Tan Y, Zhang Z, Liu X, Hem X. Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism. Cell 2002;108:837-847. (Pubitemid 34327534)
    • (2002) Cell , vol.108 , Issue.6 , pp. 837-847
    • Liu, C.1    Li, Y.2    Semenov, M.3    Han, C.4    Baeg, G.-H.5    Tan, Y.6    Zhang, Z.7    Lin, X.8    He, X.9
  • 31
    • 0036295950 scopus 로고    scopus 로고
    • Characterisation of the phosphorylation of β-catenin at the GSK-3 priming site Ser45
    • DOI 10.1016/S0006-291X(02)00485-0, PII S0006291X02004850
    • Hagen T, Vidal-pulig A. Characterisation of the phosphorylation of β-catenin at the GSK-3 priming site Ser45. Biochem Biophys Res Commun 2002;294:324-328. (Pubitemid 34694097)
    • (2002) Biochemical and Biophysical Research Communications , vol.294 , Issue.2 , pp. 324-328
    • Hagen, T.1    Vidal-Puig, A.2
  • 32
    • 0034693230 scopus 로고    scopus 로고
    • Differential regulation of glycogen synthase kinase 3β by insulin and Wnt signaling
    • Ding VW, Chen RH, McCormick F. Differential regulation of glycogen synthase kinase 3β by insulin and Wnt signaling. J Biol Chem 2000;275:32475-32481.
    • (2000) J Biol Chem , vol.275 , pp. 32475-32481
    • Ding, V.W.1    Chen, R.H.2    McCormick, F.3
  • 33
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • DOI 10.1038/378785a0
    • Cross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmins BA. Inhibition of glycogen synthase kinase-3by insulin mediated by protein kinase B. Nature 1995;378:785-789. (Pubitemid 26004411)
    • (1995) Nature , vol.378 , Issue.6559 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 34
    • 0034969088 scopus 로고    scopus 로고
    • A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation
    • DOI 10.1016/S1097-2765(01)00253-2
    • Frame S, Cohen P, Biondi RM. A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation. Mol Cell 2001;7:1321-1327. (Pubitemid 32607364)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1321-1327
    • Frame, S.1    Cohen, P.2    Biondi, R.M.3
  • 35
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3β: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH. Crystal structure of glycogen synthase kinase 3β: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 2001;105:721-732.
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Young, N.4    Good, V.5    Dale, T.C.6    Pearl, L.H.7
  • 38
    • 0032493729 scopus 로고    scopus 로고
    • Role of glycogen synthase kinase-3 in the phosphatidylinositol 3- Kinase/Akt cell survival pathway
    • DOI 10.1074/jbc.273.32.19929
    • Pap M, Cooper GM. Role of glycogen synthase kinase-3 in the phosphatidylinositol 3-kinase/Akt cell survival pathway. J Biol Chem 1998;273:19929-19932. (Pubitemid 28377539)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 19929-19932
    • Pap, M.1    Cooper, G.M.2
  • 40
    • 33645780012 scopus 로고    scopus 로고
    • E230Q mutation of the catalytic subunit of cAMP-dependent protein kinase affects local structure and the binding of peptide inhibitor
    • Ung MU, Lu BZ, McCammon JA. E230Q mutation of the catalytic subunit of cAMP-dependent protein kinase affects local structure and the binding of peptide inhibitor. Biopolymers 2006;81:428-439.
    • (2006) Biopolymers , vol.81 , pp. 428-439
    • Ung, M.U.1    Lu, B.Z.2    McCammon, J.A.3
  • 41
    • 34248578077 scopus 로고    scopus 로고
    • Insights into unbinding mechanisms upon two mutations investigated by molecular dynamics study of GSK3β-axin complex: Role of packing hydrophobic residues
    • DOI 10.1002/prot.21359
    • Zhang N, Jiang YJ, Zou JW, Zhuang SL, Jin HX, Yu QS. Insights into unbinding mechanisms upon two mutations investigated by molecular dynamics study of GSK3α-Axin complex: role of packing hydrophobic residues. Proteins 2007;67:941-949. (Pubitemid 46753941)
    • (2007) Proteins: Structure, Function and Genetics , vol.67 , Issue.4 , pp. 941-949
    • Zhang, N.1    Jiang, Y.2    Zou, J.3    Zhuang, S.4    Jin, H.5    Yu, Q.6
  • 43
    • 0003797555 scopus 로고    scopus 로고
    • St. Louis, MO: Tripos Associates Inc.
    • Sybyl Version 6.8. St. Louis, MO: Tripos Associates Inc.; 2001.
    • (2001) Sybyl Version 6.8
  • 45
    • 15744387842 scopus 로고    scopus 로고
    • Competition between intramolecular hydrogen bonds and solvation in phosphorylated peptides: Simulations with explicit and implicit solvent
    • Wong SE, Bernacki K, Jacobson M. Competition between intramolecular hydrogen bonds and solvation in phosphorylated peptides: simulations with explicit and implicit solvent. J Phys Chem B 2005;109:5249-5258.
    • (2005) J Phys Chem B , vol.109 , pp. 5249-5258
    • Wong, S.E.1    Bernacki, K.2    Jacobson, M.3
  • 46
    • 33644753023 scopus 로고    scopus 로고
    • AMBER force-field parameters for phosphorylated amino acids in different protonation states: Phosphoserine, phosphothreonine, phosphotyrosine, and phosphohistidine
    • DOI 10.1007/s00894-005-0028-4
    • Homeyer N, Horn AH, Lanig H, Sticht H. AMBER force field parameters for phosphorylated amino acids in different protonation states: phosphoserine, phosphothreonine, phosphotyrosine and phosphohistidine. J Mol Model 2006;12:281-289. (Pubitemid 43337197)
    • (2006) Journal of Molecular Modeling , vol.12 , Issue.3 , pp. 281-289
    • Homeyer, N.1    Horn, A.H.C.2    Lanig, H.3    Sticht, H.4
  • 47
    • 0037495965 scopus 로고    scopus 로고
    • Development of polyphosphate parameters for use with the AMBER force field
    • Meagher KL, Redman LT, Carlson HA. Development of polyphosphate parameters for use with the AMBER force field. J Comput Chem 2003;24:1016-1025.
    • (2003) J Comput Chem , vol.24 , pp. 1016-1025
    • Meagher, K.L.1    Redman, L.T.2    Carlson, H.A.3
  • 51
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 1977;23:327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 52
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle mesh Ewald: an N log(N) method for Ewald sums in large systems. J Chem Phys 1993;98:10089-10094.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10094
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 53
    • 0032560959 scopus 로고    scopus 로고
    • Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices
    • Srivivasan J, Cheatham T, III, Cieplak P, Kollman PA, Case DA. Continuum solvent studies of the stability of DNA, RNA, and phosphoramidate-DNA helices J Am Chem Soc 1998;120:9401-9409.
    • (1998) J Am Chem Soc , vol.120 , pp. 9401-9409
    • Srivivasan, J.1    Cheatham, T.2    Iii Cieplak, P.3    Kollman, P.A.4    Case, D.A.5
  • 55
    • 0000043930 scopus 로고    scopus 로고
    • Solvation free energy of biomacromolecules: Parameters for a modified generalized born model consistent with the AMBER force field
    • Jayaram B, Sprous D, Beveridge DL. Solvation free energy of biomacromolecules: parameters for a modified generalized born model consistent with the AMBER force field. J Phys Chem B 1998;102:9571-9576. (Pubitemid 128611876)
    • (1998) Journal of Physical Chemistry B , vol.102 , Issue.47 , pp. 9571-9576
    • Jayaram, B.1    Sprous, D.2    Beveridge, D.L.3
  • 56
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution: Method and error assessment
    • Gilson MK, Sharp KA, Honig BH. Calculating the electrostatic potential of molecules in solution: method and error assessment. J Comput Chem 1987;9:327-335.
    • (1987) J Comput Chem , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.H.3
  • 57
    • 0346971105 scopus 로고    scopus 로고
    • Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures
    • Feig M, Onufriev A, Lee MS, Im W, Case DA, Brooks CL, III. Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures. J Comput Chem 2004;25:265-284.
    • (2004) J Comput Chem , vol.25 , pp. 265-284
    • Feig, M.1    Onufriev, A.2    Lee, M.S.3    Im, W.4    Case, D.A.5    Brooks III, C.L.6
  • 58
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser J, Shenkin PS, Still WC. Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO). J Comput Chem 1999;20:217-230. (Pubitemid 129653030)
    • (1999) Journal of Computational Chemistry , vol.20 , Issue.2 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 59
    • 11644251375 scopus 로고    scopus 로고
    • Comparison of a GB solvation model with explicit solvent simulations: Potentials of mean force and conformational preferences of alanine dipeptide and 1,2-dichloroethane
    • Scarsi M, Apostolakis J, Caflisch A. Comparison of a GB solvation model with explicit solvent simulations: potentials of mean force and conformational preferences of alanine dipeptide and 1,2-dichloroethane. J Phys Chem B 1998;102:3637-3641. (Pubitemid 128576692)
    • (1998) Journal of Physical Chemistry B , vol.102 , Issue.18 , pp. 3637-3641
    • Scarsi, M.1    Apostolakis, J.2    Caflisch, A.3
  • 60
    • 0034811498 scopus 로고    scopus 로고
    • Use of MM-PBSA in reproducing the binding free energies to HIV-1 RT of TIBO derivatives and predicting the binding mode to HIV-1 RT of efavirenz by docking and MM-PBSA
    • DOI 10.1021/ja003834q
    • Wang J, Morin P, Wang W, Kollman PA. Use of MM-PBSA in reproducing the binding free energies to HIV-1 RT of TIBO derivatives and predicting the binding mode to HIV-1 RT of efavirenz by docking and MM-PBSA. J Am Chem Soc 2001;123:5221-5230. (Pubitemid 32910665)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.22 , pp. 5221-5230
    • Wang, J.1    Morin, P.2    Wang, W.3    Kollman, P.A.4
  • 61
    • 0034084991 scopus 로고    scopus 로고
    • Combined molecular mechanical and continuum solvent approach (MM- PBSA/GBSA) to predict ligand binding
    • DOI 10.1023/A:1008763014207
    • Massova I, Kollman PA. Combined molecular mechanical and continuum solvent approach (MM-PBSA/GBSA) to predict ligand binding. Persp Drug Disc Des 2000;18:113-135. (Pubitemid 30191024)
    • (2000) Perspectives in Drug Discovery and Design , vol.18 , pp. 113-135
    • Massova, I.1    Kollman, P.A.2
  • 65
    • 0028865669 scopus 로고
    • Kinetic analysis of cAMP-dependent protein kinase: Mutations at histidine 87 affect peptide binding and pH dependence
    • Cox S, Taylor SS. Kinetic analysis of cAMP-dependent protein kinase: mutations at histidine 87 affect peptide binding and pH dependence. Biochemistry 1995;34:16203-16209.
    • (1995) Biochemistry , vol.34 , pp. 16203-16209
    • Cox, S.1    Taylor, S.S.2
  • 66
    • 3042584697 scopus 로고    scopus 로고
    • Structural modes of stabilization of permissive phosphorylation sites in protein kinases: Distinct strategies in Ser/Thr and Tyr kinases
    • DOI 10.1016/j.jmb.2004.04.043, PII S002228360400484X
    • Preethi KG, Srinivasan N. Structural modes of stabilization of permissive phosphorylation sites in protein kinases: distinct strategies in Ser/Thr and Tyr kinases A. J Mol Biol 2004;339:1025-1039. (Pubitemid 39303246)
    • (2004) Journal of Molecular Biology , vol.339 , Issue.5 , pp. 1025-1039
    • Krupa, A.1    Preethi, G.2    Srinivasan, N.3
  • 67
    • 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 RT, Hemmer W, Taylor SS. 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 2000;39:8325-8332.
    • (2000) Biochemistry , vol.39 , pp. 8325-8332
    • Aimes, R.T.1    Hemmer, W.2    Taylor, S.S.3
  • 68
    • 0032568629 scopus 로고    scopus 로고
    • Kinetic analyses of mutations in the glycine-rich loop of cAMP-dependent protein kinase
    • DOI 10.1021/bi972987w
    • Grant B, Hemmer W, Tsigelny I, Adams JA, Taylor SS. Kinetic analyses of mutations in the glycine-rich loop of cAMP-dependent protein kinase. Biochemistry 1998;37:7708-7715. (Pubitemid 28248629)
    • (1998) Biochemistry , vol.37 , Issue.21 , pp. 7708-7715
    • Grant, B.D.1    Hemmer, W.2    Tsigelny, I.3    Adams, J.A.4    Taylor, S.S.5
  • 69
    • 33846632794 scopus 로고    scopus 로고
    • Role of phosphorylated Thr-197 in the catalytic subunit of cAMP-dependent protein kinase
    • Jin HX, Wu TX, Jiang YJ, Zou JW, Zhuang SL, Mao X, Yu QS. Role of phosphorylated Thr-197 in the catalytic subunit of cAMP-dependent protein kinase. J Mol Struct 2007;805:9-15.
    • (2007) J Mol Struct , vol.805 , pp. 9-15
    • Jin, H.X.1    Wu, T.X.2    Jiang, Y.J.3    Zou, J.W.4    Zhuang, S.L.5    Mao, X.6    Yu, Q.S.7
  • 70
    • 13244287683 scopus 로고    scopus 로고
    • The mechanism of inhibition of the cyclin-dependent kinase-2 as revealed by the molecular dynamics study on the complex CDK2 with the peptide substrate HHASPRK
    • DOI 10.1110/ps.04959705
    • Bártová I, Otyepka M, Kr̂îẑ Z, Koĉa J. The mechanism of inhibition of the cyclin-dependent kinase-2 as revealed by the molecular dynamics study on the complex CDK2 with the peptide substrate HHASPRKIVETA. Protein Sci 2005;14:445-451. (Pubitemid 40194597)
    • (2005) Protein Science , vol.14 , Issue.2 , pp. 445-451
    • Bartova, I.1    Otyepka, M.2    Kriz, Z.3    Koca, J.4
  • 71
    • 2442667660 scopus 로고    scopus 로고
    • Activation and inhibition of cyclin-dependent kinase-2 by phosphorylation; a molecular dynamics study reveals the functional importance of the glycine-rich loop
    • DOI 10.1110/ps.03578504
    • Bártová I, Otyepka M, Kr̂îẑ Z, Koĉa J. Activation and inhibition of cyclin-dependent kinase-2 by phosphorylation, a molecular dynamics study reveals the functional importance of the glycine-rich loop. Protein Sci 2004;13:1449-1457. (Pubitemid 38669233)
    • (2004) Protein Science , vol.13 , Issue.6 , pp. 1449-1457
    • Bartova, I.1    Otyepka, M.2    Kriz, Z.3    Koca, J.4
  • 73
    • 0030945871 scopus 로고    scopus 로고
    • Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors
    • DOI 10.1126/science.276.5314.955
    • Mohammadi M, McMahon G, Sun L, Tang C, Hirth P, Yeh BK, Hubbar SR, Schlessinger J. Structures of the tyrosine kinase domain of fibroblastgrowth factor receptor in complex with inhibitors. Science 1997;276:955-960. (Pubitemid 27209095)
    • (1997) Science , vol.276 , Issue.5314 , pp. 955-960
    • Mohammadi, M.1    McMahon, G.2    Sun, L.3    Tang, C.4    Hirth, P.5    Yeh, B.K.6    Hubbard, S.R.7    Schlessinger, J.8
  • 74
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard SR, Wei L, Ellis L, Hendrickson WA. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 1994;372:746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 75
    • 17144420076 scopus 로고    scopus 로고
    • Molecular motions of human cyclin-dependent kinase 2
    • DOI 10.1074/jbc.M407371200
    • Barrett CP, Noble MEM. Molecular motions of human Cyclin-dependent kinase 2. J Biol Chem 2005;80:13993-14005. (Pubitemid 40517301)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13993-14005
    • Barrett, C.P.1    Noble, M.E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.