메뉴 건너뛰기




Volumn 67, Issue 4, 2007, Pages 1048-1059

Recognition of Cdk2 by Cdk7

Author keywords

Cell cycle; Computational docking; Cyclin dependent kinases; Molecular surface recognition; Phosphorylation; Site directed mutagenesis

Indexed keywords

CYCLIN A; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 7;

EID: 34248583324     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21370     Document Type: Article
Times cited : (25)

References (50)
  • 1
    • 0036710767 scopus 로고    scopus 로고
    • Pharmacological inhibitors of cyclin-dependent kinases
    • Knockaert M, Greengard P, Meijer L. Pharmacological inhibitors of cyclin-dependent kinases. Trends Pharmacol Sci 2002;23:417-425.
    • (2002) Trends Pharmacol Sci , vol.23 , pp. 417-425
    • Knockaert, M.1    Greengard, P.2    Meijer, L.3
  • 2
    • 1642323740 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Insights into drug design from structure
    • Noble ME, Endicott JA, Johnson LN. Protein kinase inhibitors: insights into drug design from structure. Science 2004;303:1800-1805.
    • (2004) Science , vol.303 , pp. 1800-1805
    • Noble, M.E.1    Endicott, J.A.2    Johnson, L.N.3
  • 3
    • 33645802169 scopus 로고    scopus 로고
    • Cyclin-dependent kinase pathways as targets for cancer treatment
    • Shapiro GI. Cyclin-dependent kinase pathways as targets for cancer treatment. J Clin Oncol 2006;24:1770-1783.
    • (2006) J Clin Oncol , vol.24 , pp. 1770-1783
    • Shapiro, G.I.1
  • 4
    • 0027185999 scopus 로고
    • CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15
    • Solomon MJ, Harper JW, Shuttleworth J. CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15: EMBO J 1993;12:3133-3142.
    • (1993) EMBO J , vol.12 , pp. 3133-3142
    • Solomon, M.J.1    Harper, J.W.2    Shuttleworth, J.3
  • 5
    • 0027007963 scopus 로고
    • Role of phosphorylation in p34cdc2 activation: Identification of an activating kinase
    • Solomon MJ, Lee T, Kirschner MW. Role of phosphorylation in p34cdc2 activation: identification of an activating kinase. Mol Biol Cell 1992;3:13-27.
    • (1992) Mol Biol Cell , vol.3 , pp. 13-27
    • Solomon, M.J.1    Lee, T.2    Kirschner, M.W.3
  • 6
    • 0027296041 scopus 로고
    • The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues
    • Fesquet D, Labbe' J-C, Derancourt J, Capony J-P, Galas S, Girard F, Lorca T, Shuttleworth J, Doree M, Cavadore JC. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues. EMBO J 1993;12:3111-3121.
    • (1993) EMBO J , vol.12 , pp. 3111-3121
    • Fesquet, D.1    Labbe', J.-C.2    Derancourt, J.3    Capony, J.-P.4    Galas, S.5    Girard, F.6    Lorca, T.7    Shuttleworth, J.8    Doree, M.9    Cavadore, J.C.10
  • 7
    • 0027251024 scopus 로고
    • The cdc2-related protein p40MO15 is the catalytic subunit of a protein kinase that can activate p33cdk2 and p34cdc2
    • Poon RYC, Yamashita K, Adamczewski JP, Hunt T, Shuttleworth J. The cdc2-related protein p40MO15 is the catalytic subunit of a protein kinase that can activate p33cdk2 and p34cdc2. EMBO J 1993;12:3123-3132.
    • (1993) EMBO J , vol.12 , pp. 3123-3132
    • Poon, R.Y.C.1    Yamashita, K.2    Adamczewski, J.P.3    Hunt, T.4    Shuttleworth, J.5
  • 8
    • 0027994603 scopus 로고
    • A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase
    • Fisher RP, Morgan DO. A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. Cell 1994;78:713-724.
    • (1994) Cell , vol.78 , pp. 713-724
    • Fisher, R.P.1    Morgan, D.O.2
  • 9
    • 0028270189 scopus 로고
    • Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase
    • Kato J-Y, Matsuoka M, Storm DK, Sherr CJ. Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase. Mol Cell Biol 1994;14:2713-2721.
    • (1994) Mol Cell Biol , vol.14 , pp. 2713-2721
    • Kato, J.-Y.1    Matsuoka, M.2    Storm, D.K.3    Sherr, C.J.4
  • 10
    • 0027943714 scopus 로고
    • Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-associated kinase
    • Matsuoka M, Kato J-Y, Fisher RP, Morgan DO, Sherr CJ. Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-associated kinase. Mol Cell Biol 1994;14:7265-7275.
    • (1994) Mol Cell Biol , vol.14 , pp. 7265-7275
    • Matsuoka, M.1    Kato, J.-Y.2    Fisher, R.P.3    Morgan, D.O.4    Sherr, C.J.5
  • 12
    • 0028807103 scopus 로고
    • Alternative mechanism of CAK assembly require an assembly factor or an activating kinase
    • Fisher RP, Jin P, Chamberlin HM, Morgan DO. Alternative mechanism of CAK assembly require an assembly factor or an activating kinase. Cell 1995;83:47-57.
    • (1995) Cell , vol.83 , pp. 47-57
    • Fisher, R.P.1    Jin, P.2    Chamberlin, H.M.3    Morgan, D.O.4
  • 13
    • 0031016629 scopus 로고    scopus 로고
    • Dual phosphorylation of the T-loop in cdk7: Its role in controlling cyclin H binding and CAK activity
    • Martinez A-M, Afshar M, Martin F, Cavadore J-C, Labbé J-C, Doree M. Dual phosphorylation of the T-loop in cdk7: its role in controlling cyclin H binding and CAK activity. EMBO J 1997;16:343-354.
    • (1997) EMBO J , vol.16 , pp. 343-354
    • Martinez, A.-M.1    Afshar, M.2    Martin, F.3    Cavadore, J.-C.4    Labbé, J.-C.5    Doree, M.6
  • 14
    • 0034747803 scopus 로고    scopus 로고
    • Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop
    • Garrett S, Barton WA, Knights R, Jin P, Morgan DO, Fisher RP. Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop. Mol Cell Biol 2001;21:88-99.
    • (2001) Mol Cell Biol , vol.21 , pp. 88-99
    • Garrett, S.1    Barton, W.A.2    Knights, R.3    Jin, P.4    Morgan, D.O.5    Fisher, R.P.6
  • 16
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown NR, Noble ME, Endicott JA, Johnson LN. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat Cell Biol 1999;1:438-443.
    • (1999) Nat Cell Biol , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.2    Endicott, J.A.3    Johnson, L.N.4
  • 17
    • 0028983384 scopus 로고
    • p107 uses a p21CIP1-related domain to bind cyclin/cdk2 and regulate interactions with E2F
    • Zhu L, Harlow E, Dynlacht BD. p107 uses a p21CIP1-related domain to bind cyclin/cdk2 and regulate interactions with E2F. Genes Dev 1995;9:1740-1752.
    • (1995) Genes Dev , vol.9 , pp. 1740-1752
    • Zhu, L.1    Harlow, E.2    Dynlacht, B.D.3
  • 18
    • 0029928180 scopus 로고    scopus 로고
    • Analysis of wild-type and mutant p21WAF-1 gene activities
    • Lin J, Reichner C, Wu X, Levine AJ. Analysis of wild-type and mutant p21WAF-1 gene activities. Mol Cell Biol 1996;16:1786-1793.
    • (1996) Mol Cell Biol , vol.16 , pp. 1786-1793
    • Lin, J.1    Reichner, C.2    Wu, X.3    Levine, A.J.4
  • 19
    • 0030990095 scopus 로고    scopus 로고
    • Specific regulation of E2F family members by cyclin-dependent kinases
    • Dynlacht BD, Moberg K, Lees JA, Harlow E, Zhu L. Specific regulation of E2F family members by cyclin-dependent kinases. Mol Cell Biol 1997;17:3867-3875.
    • (1997) Mol Cell Biol , vol.17 , pp. 3867-3875
    • Dynlacht, B.D.1    Moberg, K.2    Lees, J.A.3    Harlow, E.4    Zhu, L.5
  • 22
    • 0034647433 scopus 로고    scopus 로고
    • The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A
    • Luciani MG, Hutchins JR, Zheleva D, Hupp TR. The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A. J Mol Biol 2000;300:503-518.
    • (2000) J Mol Biol , vol.300 , pp. 503-518
    • Luciani, M.G.1    Hutchins, J.R.2    Zheleva, D.3    Hupp, T.R.4
  • 23
    • 0032802393 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Inhibition and substrate recognition
    • Endicott JA, Noble ME, Tucker JA. Cyclin-dependent kinases: inhibition and substrate recognition. Curr Opin Struct Biol 1999;9:738-744.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 738-744
    • Endicott, J.A.1    Noble, M.E.2    Tucker, J.A.3
  • 24
    • 0029973557 scopus 로고    scopus 로고
    • Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors
    • Adams PD, Sellers WR, Sharma SK, Wu AD, Nalin CM, Kaelin WG Jr. Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors. Mol Cell Biol 1996;16:6623-6633.
    • (1996) Mol Cell Biol , vol.16 , pp. 6623-6633
    • Adams, P.D.1    Sellers, W.R.2    Sharma, S.K.3    Wu, A.D.4    Nalin, C.M.5    Kaelin Jr., W.G.6
  • 25
  • 27
    • 0032167631 scopus 로고    scopus 로고
    • Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A
    • Schulman BA, Lindstrom DL, Harlow E. Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A. Proc Natl Acad Sci USA 1998;95:10453-10458.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10453-10458
    • Schulman, B.A.1    Lindstrom, D.L.2    Harlow, E.3
  • 28
    • 7944231428 scopus 로고    scopus 로고
    • The crystal structure of human CDK7 and its protein recognition properties
    • Lolli G, Lowe ED, Brown NR, Johnson LN. The crystal structure of human CDK7 and its protein recognition properties. Structure 2004;12:2067-2079.
    • (2004) Structure , vol.12 , pp. 2067-2079
    • Lolli, G.1    Lowe, E.D.2    Brown, N.R.3    Johnson, L.N.4
  • 29
    • 0034725689 scopus 로고    scopus 로고
    • Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcrition activities
    • Busso D, Keriel A, Sandrock B, Poterszman A, Gileadi O, Egly J-M. Distinct regions of MAT1 regulate cdk7 kinase and TFIIH transcrition activities. J Biol Chem 2000;275:22815-22823.
    • (2000) J Biol Chem , vol.275 , pp. 22815-22823
    • Busso, D.1    Keriel, A.2    Sandrock, B.3    Poterszman, A.4    Gileadi, O.5    Egly, J.-M.6
  • 31
    • 0033562633 scopus 로고    scopus 로고
    • Use of pair potentials across protein interfaces in screening predicted docked complexes
    • Moont G, Gabb HA, Sternberg MJ. Use of pair potentials across protein interfaces in screening predicted docked complexes. Proteins 1999;35:364-373.
    • (1999) Proteins , vol.35 , pp. 364-373
    • Moont, G.1    Gabb, H.A.2    Sternberg, M.J.3
  • 32
    • 0031565730 scopus 로고    scopus 로고
    • Modelling protein docking using shape complementarity, electrostatics and biochemical information
    • Gabb HA, Jackson RM, Sternberg MJ. Modelling protein docking using shape complementarity, electrostatics and biochemical information. J Mol Biol 1997;272:106-120.
    • (1997) J Mol Biol , vol.272 , pp. 106-120
    • Gabb, H.A.1    Jackson, R.M.2    Sternberg, M.J.3
  • 33
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Mod 2001;7:306-317.
    • (2001) J Mol Mod , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 34
    • 0028103275 scopus 로고
    • The CCP4 (collaborative computational project number 4) suite: Programmes for protein crystallography. Acta Cryst D Biol Crystallogr
    • 4
    • CCP4. The CCP4 (collaborative computational project number 4) suite: programmes for protein crystallography. Acta Cryst D Biol Crystallogr 1994;50:760-763.
    • (1994) , vol.50 , pp. 760-763
    • CCP1
  • 36
    • 0035265679 scopus 로고    scopus 로고
    • Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2
    • Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D. Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Mol Cell 2001;7:615-626.
    • (2001) Mol Cell , vol.7 , pp. 615-626
    • Song, H.1    Hanlon, N.2    Brown, N.R.3    Noble, M.E.4    Johnson, L.N.5    Barford, D.6
  • 37
    • 33646195686 scopus 로고    scopus 로고
    • Detection of protein assemblies in crystals
    • Berthold MR, Glen R, Diederichs K, Kohlbacher O, Fischer I, editors, Berlin, Heidelberg: Springer-Verlag;
    • Krissinel E, Henrick K. Detection of protein assemblies in crystals. In: Berthold MR, Glen R, Diederichs K, Kohlbacher O, Fischer I., editors. Lecture Notes in Computer Science, CompLife, Vol.3695. Berlin, Heidelberg: Springer-Verlag; 2005. pp 163-174.
    • (2005) Lecture Notes in Computer Science, CompLife , vol.3695 , pp. 163-174
    • Krissinel, E.1    Henrick, K.2
  • 38
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi M, Schlessinger J, Hubbard SR. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 1996;86:577-587.
    • (1996) Cell , vol.86 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 39
    • 0035045092 scopus 로고    scopus 로고
    • Prediction of the structure of human Janus kinase 2 (JAK2) comprising the two carboxy-terminal domains reveals a mechanism for autoregulation
    • Lindauer K, Loerting T, Liedl KR, Kroemer RT. Prediction of the structure of human Janus kinase 2 (JAK2) comprising the two carboxy-terminal domains reveals a mechanism for autoregulation. Protein Eng 2001;14:27-37.
    • (2001) Protein Eng , vol.14 , pp. 27-37
    • Lindauer, K.1    Loerting, T.2    Liedl, K.R.3    Kroemer, R.T.4
  • 41
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein/protein interfaces
    • McCoy AJ, Chandana Epa V, Colman PM. Electrostatic complementarity at protein/protein interfaces. J Mol Biol 1997;268:570-584.
    • (1997) J Mol Biol , vol.268 , pp. 570-584
    • McCoy, A.J.1    Chandana Epa, V.2    Colman, P.M.3
  • 42
    • 14844307019 scopus 로고    scopus 로고
    • The structure of cyclin E1/CDK2: Implications for CDK2 activation and CDK2-independent roles
    • Honda R, Lowe ED, Dubinina E, Skamnaki V, Cook A, Brown NR, Johnson LN. The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles. EMBO J 2005;24:452-463.
    • (2005) EMBO J , vol.24 , pp. 452-463
    • Honda, R.1    Lowe, E.D.2    Dubinina, E.3    Skamnaki, V.4    Cook, A.5    Brown, N.R.6    Johnson, L.N.7
  • 43
    • 0034630762 scopus 로고    scopus 로고
    • The N-terminal domains of cyclin-dependent kinase inhibitory proteins block the phosphorylation of cdk2/Cyclin E by the CDK-activating kinase
    • Rank KB, Evans DB, Sharma SK. The N-terminal domains of cyclin-dependent kinase inhibitory proteins block the phosphorylation of cdk2/Cyclin E by the CDK-activating kinase. Biochem Biophys Res Commun 2000;271:469-473.
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 469-473
    • Rank, K.B.1    Evans, D.B.2    Sharma, S.K.3
  • 46
    • 0242353366 scopus 로고    scopus 로고
    • Cdk7 functions as a cdk5 activating kinase in brain
    • Rosales J, Han B, Lee KY. Cdk7 functions as a cdk5 activating kinase in brain. Cell Physiol Biochem 2003;13:285-296.
    • (2003) Cell Physiol Biochem , vol.13 , pp. 285-296
    • Rosales, J.1    Han, B.2    Lee, K.Y.3
  • 49
    • 0029147732 scopus 로고
    • Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase
    • Aprelikova O, Xiong Y, Liu ET. Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase. J Biol Chem 1995;270:18195-18197.
    • (1995) J Biol Chem , vol.270 , pp. 18195-18197
    • Aprelikova, O.1    Xiong, Y.2    Liu, E.T.3
  • 50
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 1996;382:325-331.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.