메뉴 건너뛰기




Volumn 13, Issue 6, 2004, Pages 1449-1457

Activation and inhibition of cyclin-dependent kinase-2 by phosphorylation; a molecular dynamics study reveals the functional importance of the glycine-rich loop

Author keywords

CDK regulation; Cell cycle; Phosphorylated tyrosine; Threonine

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYCLIN A; CYCLIN DEPENDENT KINASE 2; GLYCINE; THREONINE; TYROSINE;

EID: 2442667660     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03578504     Document Type: Article
Times cited : (78)

References (43)
  • 1
    • 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, R.T., Hemmer, W., and Taylor, S.S. 2000. 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 39: 8325-8332.
    • (2000) Biochemistry , vol.39 , pp. 8325-8332
    • Aimes, R.T.1    Hemmer, W.2    Taylor, S.S.3
  • 2
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown, N.R., Noble, M.E.M., Endicott, J.A., and Johnson, L.N. 1999. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat. Cell Biol. 1: 438-443.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.M.2    Endicott, J.A.3    Johnson, L.N.4
  • 4
    • 0032751695 scopus 로고    scopus 로고
    • Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
    • Cheng, A., Ross, K.E., Kaldis, P., and Solomon, M.J. 1999. Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes Dev. 13: 2946-2957.
    • (1999) Genes Dev. , vol.13 , pp. 2946-2957
    • Cheng, A.1    Ross, K.E.2    Kaldis, P.3    Solomon, M.J.4
  • 5
    • 0034602268 scopus 로고    scopus 로고
    • Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C α and β 2 isoforms
    • Cheng, A., Kaldis, P., and Solomon, M.J. 2000. Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C α and β 2 isoforms. J. Biol. Chem. 275: 34744-34749.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34744-34749
    • Cheng, A.1    Kaldis, P.2    Solomon, M.J.3
  • 6
    • 0142135133 scopus 로고    scopus 로고
    • Differential contribution of inhibitory phosphorylation of CDC2 and CDK2 for unperturbed cell cycle control and DNA integrity checkpoints
    • Chow, J.P., Siu, W.Y., Ho, H.T., Ma, K.H., Ho, C.C., and Poon, R.Y.C. 2003. Differential contribution of inhibitory phosphorylation of CDC2 and CDK2 for unperturbed cell cycle control and DNA integrity checkpoints. J. Biol. Chem. 278: 40815-40828.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40815-40828
    • Chow, J.P.1    Siu, W.Y.2    Ho, H.T.3    Ma, K.H.4    Ho, C.C.5    Poon, R.Y.C.6
  • 7
    • 0037062580 scopus 로고    scopus 로고
    • Structural studies on phospho-CDK2/Cyclin A bound to nitrate, a transition state analogue: Implications for the protein kinase mechanism
    • Cook, A., Lowe, E.D., Chrysina, E.D., Skamnaki, V.T., Oikonomakos, N.G., and Johnson, L.N. 2002. Structural studies on phospho-CDK2/Cyclin A bound to nitrate, a transition state analogue: Implications for the protein kinase mechanism. Biochemistry 41: 7301-7311.
    • (2002) Biochemistry , vol.41 , pp. 7301-7311
    • Cook, A.1    Lowe, E.D.2    Chrysina, E.D.3    Skamnaki, V.T.4    Oikonomakos, N.G.5    Johnson, L.N.6
  • 9
    • 0346101798 scopus 로고    scopus 로고
    • Phosphorylations of cyclin-dependent kinase 2 revisited using two-dimensional gel electrophoresis
    • Coulonval, K., Bockstaele, L., Paternot, S., and Roger, P.P. 2003. Phosphorylations of cyclin-dependent kinase 2 revisited using two-dimensional gel electrophoresis. J. Biol. Chem. 278: 52052-52060.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52052-52060
    • Coulonval, K.1    Bockstaele, L.2    Paternot, S.3    Roger, P.P.4
  • 11
    • 0032802393 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Inhibition and substrate recognition
    • Endicott, J.A., Noble, M.E.M., and Tucker, J.A. 1999. Cyclin-dependent kinases: Inhibition and substrate recognition. Curr. Opin. Struct. Biol. 9: 738-744.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 738-744
    • Endicott, J.A.1    Noble, M.E.M.2    Tucker, J.A.3
  • 13
    • 0026713875 scopus 로고
    • Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15
    • Gu, Y., Rosenblatt, J., and Morgan, D.O. 1992. Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15. EMBO J. 11: 3995-4005.
    • (1992) EMBO J. , vol.11 , pp. 3995-4005
    • Gu, Y.1    Rosenblatt, J.2    Morgan, D.O.3
  • 14
    • 0035808444 scopus 로고    scopus 로고
    • Kinetic basis for activation of CDK2/Cyclin A by phosphorylation
    • Hagopian, J.C., Kirtley, M.P., and Stevenson, L.M. 2001. Kinetic basis for activation of CDK2/Cyclin A by phosphorylation. J. Biol. Chem. 276: 275-280.
    • (2001) J. Biol. Chem. , vol.276 , pp. 275-280
    • Hagopian, J.C.1    Kirtley, M.P.2    Stevenson, L.M.3
  • 15
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S. and Quinn, A.M. 1991. Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200: 38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.1    Quinn, A.M.2
  • 16
    • 0030859238 scopus 로고    scopus 로고
    • Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase
    • 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.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16946-16954
    • Hemmer, W.1    McGlone, M.2    Tsigelny, I.3    Taylor, S.S.4
  • 17
    • 0029819179 scopus 로고    scopus 로고
    • A predictive scale for evaluation cyclin-dependent kinase substrates. A comparison of p34cdc2 and p33cdk2
    • Holmes, J.K. and Solomon, M.J. 1996. A predictive scale for evaluation cyclin-dependent kinase substrates. A comparison of p34cdc2 and p33cdk2. J. Biol. Chem. 271: 25240-25246.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25240-25246
    • Holmes, J.K.1    Solomon, M.J.2
  • 18
    • 0035724495 scopus 로고    scopus 로고
    • The role of Thr160 phosphorylation of Cdk2 in substrate recognition
    • -. 2001. The role of Thr160 phosphorylation of Cdk2 in substrate recognition. Eur. J. Biochem. 268: 4647-4652.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4647-4652
  • 20
    • 0033590627 scopus 로고    scopus 로고
    • Cell cycle start from quiescence controlled by tyrosine phosphorylation of Cdk4
    • Jinno, S., Hung, S.C., and Okayama, H. 1999. Cell cycle start from quiescence controlled by tyrosine phosphorylation of Cdk4. Oncogene 18: 565-571.
    • (1999) Oncogene , vol.18 , pp. 565-571
    • Jinno, S.1    Hung, S.C.2    Okayama, H.3
  • 21
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • Johnson, L.N. and Lewis, R.J. 2001. Structural basis for control by phosphorylation. Chem. Rev. 101: 2209-2242.
    • (2001) Chem. Rev. , vol.101 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 23
    • 0036710767 scopus 로고    scopus 로고
    • Pharmacological inhibitors of cyclin-dependent kinases
    • Knockaert, M., Greengard, P., and Meijer, L. 2002. Pharmacological inhibitors of cyclin-dependent kinases. Trends Pharmacol. Sci. 23: 417-425.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 417-425
    • Knockaert, M.1    Greengard, P.2    Meijer, L.3
  • 24
    • 0026590397 scopus 로고
    • A graphics program for the analysis and display of molecular dynamics trajectories
    • Laaksonen, L. 1992. A graphics program for the analysis and display of molecular dynamics trajectories. J. Mol. Graph. 10: 33-34.
    • (1992) J. Mol. Graph. , vol.10 , pp. 33-34
    • Laaksonen, L.1
  • 25
    • 0037417767 scopus 로고    scopus 로고
    • MAP kinases and CDKs: Kinetic basis for catalytic activation
    • Lew, J. 2003. MAP kinases and CDKs: Kinetic basis for catalytic activation. Biochemistry 42: 849-856.
    • (2003) Biochemistry , vol.42 , pp. 849-856
    • Lew, J.1
  • 26
    • 0030561611 scopus 로고    scopus 로고
    • The dynamics of cyclin dependent kinase structure
    • Morgan, D.O. 1996. The dynamics of cyclin dependent kinase structure. Curr. Opin. Cell Biol. 8: 767-772.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 767-772
    • Morgan, D.O.1
  • 27
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • -. 1997. Cyclin-dependent kinases: Engines, clocks, and microprocessors. Annu. Rev. Cell Dev. Biol. 13: 261-291.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 261-291
  • 28
    • 0037189530 scopus 로고    scopus 로고
    • Kinetic mechanism of activation of the Cdk2/Cyclin A complex
    • Morris, M.C., Gondeau, C., Tainer, J.A., and Divita, G. 2002. Kinetic mechanism of activation of the Cdk2/Cyclin A complex. J. Biol. Chem. 277: 23847-23853.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23847-23853
    • Morris, M.C.1    Gondeau, C.2    Tainer, J.A.3    Divita, G.4
  • 29
    • 1842866544 scopus 로고    scopus 로고
    • Dynamics and binding modes of free cdk2 and its two complexes with inhibitors studied by computer simulations
    • Otyepka, M., Kříž, Z., and Koča, J. 2002. Dynamics and binding modes of free cdk2 and its two complexes with inhibitors studied by computer simulations. J. Biomol. Struct. Dynam. 20: 141-154.
    • (2002) J. Biomol. Struct. Dynam. , vol.20 , pp. 141-154
    • Otyepka, M.1    Kříž, Z.2    Koča, J.3
  • 30
    • 0344942222 scopus 로고    scopus 로고
    • New York University School of Medicine, New York
    • Pagano, M. 1998. Cell cycle control. New York University School of Medicine, New York.
    • (1998) Cell Cycle Control
    • Pagano, M.1
  • 31
    • 0029562951 scopus 로고
    • Molecular dynamics simulation of E. coli ribonuclease H1 in solution: Correlation with NMR and X-ray data and insights into biological function
    • Philippopoulos, M. and Lim, C. 1995. Molecular dynamics simulation of E. coli ribonuclease H1 in solution: Correlation with NMR and X-ray data and insights into biological function. J. Mol. Biol. 254: 771-792.
    • (1995) J. Mol. Biol. , vol.254 , pp. 771-792
    • Philippopoulos, M.1    Lim, C.2
  • 32
    • 0028970682 scopus 로고
    • Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin
    • Poon, R.Y.C. and Hunter, T. 1995. Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin. Science 270: 90-93.
    • (1995) Science , vol.270 , pp. 90-93
    • Poon, R.Y.C.1    Hunter, T.2
  • 33
    • 0035253383 scopus 로고    scopus 로고
    • Specifity of natural and artificial substrates for human CDC25A
    • Rudolph, J., Epstein, D.M., Parker, L., and Eckstein, J. 2001. Specifity of natural and artificial substrates for human CDC25A. Anal. Biochem. 289: 43-51.
    • (2001) Anal. Biochem. , vol.289 , pp. 43-51
    • Rudolph, J.1    Epstein, D.M.2    Parker, L.3    Eckstein, J.4
  • 34
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase 2 activation by phosphorylation
    • Russo, A.A., Jeffrey, P.D., and Pavletich, N.P. 1996. Structural basis of cyclin-dependent kinase 2 activation by phosphorylation. Nat. Struct. Biol. 3: 696-700.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 35
    • 0029090514 scopus 로고
    • Multiple modes of ligand recognition: Crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopenthenyladenine
    • Schulze-Gahmen, U., Brandsen, J., Jones, H.D., Morgan, D., Meijer, L., Veselý, J., and Kim, S.-H. 1995. Multiple modes of ligand recognition: Crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopenthenyladenine. Proteins 22: 378-391.
    • (1995) Proteins , vol.22 , pp. 378-391
    • Schulze-Gahmen, U.1    Brandsen, J.2    Jones, H.D.3    Morgan, D.4    Meijer, L.5    Veselý, J.6    Kim, S.-H.7
  • 36
    • 0027471557 scopus 로고
    • Cdc25M2 activation of cyclin-dependent kinases by dephosphorylation of threonine-14 and tyrosine-15
    • Sebastian, B., Kakizuka, A., and Hunter, T. 1993. Cdc25M2 activation of cyclin-dependent kinases by dephosphorylation of threonine-14 and tyrosine-15. Proc. Natl. Acad. Sci. 90: 3521-3524.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 3521-3524
    • Sebastian, B.1    Kakizuka, A.2    Hunter, T.3
  • 38
    • 0037007982 scopus 로고    scopus 로고
    • Activation mechanism of CDK2: Role of cyclin binding versus phosphorylation
    • Stevenson, L.M., Deal, M.S., Hagopian, J.C., and Lew, J. 2002. Activation mechanism of CDK2: Role of cyclin binding versus phosphorylation. Biochemistry 41: 8528-8534.
    • (2002) Biochemistry , vol.41 , pp. 8528-8534
    • Stevenson, L.M.1    Deal, M.S.2    Hagopian, J.C.3    Lew, J.4
  • 39
    • 0032847133 scopus 로고    scopus 로고
    • 600 ps molecular dynamics reveals stable substructures and flexible hinge points in cAMP dependent protein kinase
    • Tsigelny, I., Greenberg, J.P., Cox, S., Nichols, W.L., Taylor, S.S., and Ten Eyck, L.F. 1999. 600 ps molecular dynamics reveals stable substructures and flexible hinge points in cAMP dependent protein kinase. Biopolymers 50: 513-524.
    • (1999) Biopolymers , vol.50 , pp. 513-524
    • Tsigelny, I.1    Greenberg, J.P.2    Cox, S.3    Nichols, W.L.4    Taylor, S.S.5    Ten Eyck, L.F.6
  • 41
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang, J.M., Cieplak, P., and Kollman, P.A. 2000. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 21: 1049-1074.
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.M.1    Cieplak, P.2    Kollman, P.A.3
  • 42
    • 0029048491 scopus 로고
    • Regulation of the human WeelHu Cdk tyrosine 15-kinase during the cell cycle
    • Watanabe, N., Broome, M., and Hunter, T. 1995. Regulation of the human WeelHu Cdk tyrosine 15-kinase during the cell cycle. EMBO J. 14: 1878-1891.
    • (1995) EMBO J. , vol.14 , pp. 1878-1891
    • Watanabe, N.1    Broome, M.2    Hunter, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.