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Volumn 93, Issue 4, 1998, Pages 617-625

Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE; PHOSPHATASE; PHOSPHATASE CDC25A; PROTEIN TYROSINE PHOSPHATASE; THIOSULFATE SULFURTRANSFERASE; UNCLASSIFIED DRUG;

EID: 18144432725     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81190-3     Document Type: Article
Times cited : (270)

References (52)
  • 1
    • 0030771126 scopus 로고    scopus 로고
    • The PROSITE database, its status in 1997
    • Bairoch, A., Bucher, P., and Hofmann, K. (1997). The PROSITE database, its status in 1997. Nucleic Acids Res. 25, 217-221.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 217-221
    • Bairoch, A.1    Bucher, P.2    Hofmann, K.3
  • 2
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford, D., Flint, A.J., and Tonks, N.K. (1994). Crystal structure of human protein tyrosine phosphatase 1B. Science 263, 1397-1404.
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 3
    • 0029759927 scopus 로고    scopus 로고
    • Structural basis for inhibition of receptor protein-tyrosine phosphatase alpha by dimerization
    • Bilwes, A.M., den Hertog, J., Hunter, T., and Noel, J.P. (1996). Structural basis for inhibition of receptor protein-tyrosine phosphatase alpha by dimerization. Nature 382, 555-559.
    • (1996) Nature , vol.382 , pp. 555-559
    • Bilwes, A.M.1    Den Hertog, J.2    Hunter, T.3    Noel, J.P.4
  • 4
    • 0030836016 scopus 로고    scopus 로고
    • Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae
    • Bobrowicz, P., Wysocki, R., Owsianik, G., Goffeau, A., and Ulaszewski, S. (1997). Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Yeast 13, 819-828.
    • (1997) Yeast , vol.13 , pp. 819-828
    • Bobrowicz, P.1    Wysocki, R.2    Owsianik, G.3    Goffeau, A.4    Ulaszewski, S.5
  • 5
    • 0029981099 scopus 로고    scopus 로고
    • Sequential dephosphorylation of p34(cdc2) on Thr-14 and Tyr-15 at the prophase/metaphase transition
    • Borgne, A., and Meijer, L. (1996). Sequential dephosphorylation of p34(cdc2) on Thr-14 and Tyr-15 at the prophase/metaphase transition. J. Biol. Chem. 271, 27847-27854.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27847-27854
    • Borgne, A.1    Meijer, L.2
  • 6
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger, A.T. (1992). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Cryst. A46, 585-593.
    • (1992) Acta Cryst. , vol.A46 , pp. 585-593
    • Brünger, A.T.1
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, No. 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D50, 760-763.
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 9
    • 0029043627 scopus 로고
    • A catalytic mechanism for the dual-specific phosphatases
    • Denu, J.M., and Dixon, J.E. (1995). A catalytic mechanism for the dual-specific phosphatases. Proc. Natl. Acad. Sci. USA 92, 5910-5914.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5910-5914
    • Denu, J.M.1    Dixon, J.E.2
  • 10
    • 0025938467 scopus 로고
    • The cdc25 protein contains an intrinsic phosphatase activity
    • Dunphy, W.G., and Kumagai, A. (1991). The cdc25 protein contains an intrinsic phosphatase activity. Cell 67, 189-196.
    • (1991) Cell , vol.67 , pp. 189-196
    • Dunphy, W.G.1    Kumagai, A.2
  • 11
    • 0030034247 scopus 로고    scopus 로고
    • Identification of an essential acidic residue in Cdc25 protein phosphatase and a general three-dimensional model for a core region in protein phosphatases
    • Eckstein, J.W., Beer-Romero, P.B., and Berdo, I. (1996). Identification of an essential acidic residue in Cdc25 protein phosphatase and a general three-dimensional model for a core region in protein phosphatases. Protein Sci. 5, 5-12.
    • (1996) Protein Sci. , vol.5 , pp. 5-12
    • Eckstein, J.W.1    Beer-Romero, P.B.2    Berdo, I.3
  • 12
    • 0030296632 scopus 로고    scopus 로고
    • Structure and function of the protein tyrosine phosphatases
    • Fauman, E.B., and Saper, M.A. (1996). Structure and function of the protein tyrosine phosphatases. Trends Biochem. Sci. 21, 413-417.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 413-417
    • Fauman, E.B.1    Saper, M.A.2
  • 13
  • 14
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French, G.S., and Wilson, K.S. (1978). On the treatment of negative intensity observations. Acta Cryst. A34, 517-525.
    • (1978) Acta Cryst. , vol.A34 , pp. 517-525
    • French, G.S.1    Wilson, K.S.2
  • 15
    • 0026319225 scopus 로고
    • Specific activation of cdc25 tyrosine phosphatase by B-type cyclins: Evidence for multiple roles of mitotic cyclins
    • Galaktionov, K., and Beach, D. (1991). Specific activation of cdc25 tyrosine phosphatase by B-type cyclins: evidence for multiple roles of mitotic cyclins. Cell 67, 1181-1194.
    • (1991) Cell , vol.67 , pp. 1181-1194
    • Galaktionov, K.1    Beach, D.2
  • 16
    • 0025936510 scopus 로고
    • cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2
    • Gautier, J., Solomon, M.J., Boojer, R.N., Bazan, J.F., and Kirschner, M.W. (1991). cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2. Cell 67, 197-211.
    • (1991) Cell , vol.67 , pp. 197-211
    • Gautier, J.1    Solomon, M.J.2    Boojer, R.N.3    Bazan, J.F.4    Kirschner, M.W.5
  • 17
    • 0030299966 scopus 로고    scopus 로고
    • His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773
    • Gladysheva, T., Liu, J., and Rosen, B.P. (1996). His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773. J. Biol. Chem. 271, 33256-33260.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33256-33260
    • Gladysheva, T.1    Liu, J.2    Rosen, B.P.3
  • 18
    • 0029813504 scopus 로고    scopus 로고
    • Active site structural features for chemically modified forms of rhodanese
    • Gliubich, F., Gazerro, M., Zanotti, G., Delbono, S., Bombieri, G., and Berni, R. (1996). Active site structural features for chemically modified forms of rhodanese. J. Biol. Chem. 271, 21054-21061.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21054-21061
    • Gliubich, F.1    Gazerro, M.2    Zanotti, G.3    Delbono, S.4    Bombieri, G.5    Berni, R.6
  • 21
    • 0024959919 scopus 로고
    • Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis
    • Gould, K.L., and Nurse, P. (1989). Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 342, 39-45.
    • (1989) Nature , vol.342 , pp. 39-45
    • Gould, K.L.1    Nurse, P.2
  • 22
    • 0025945823 scopus 로고
    • Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate
    • Guan, K.L., and Dixon, J.E. (1991). Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate. J. Biol. Chem. 266, 17026-17030.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17026-17030
    • Guan, K.L.1    Dixon, J.E.2
  • 23
    • 0025865103 scopus 로고
    • A Tyr/Ser protein phosphatase encoded by a vaccinia virus
    • Guan, K., Broyles, S.S., and Dixon, J.E. (1991). A Tyr/Ser protein phosphatase encoded by a vaccinia virus. Nature 350, 359-362.
    • (1991) Nature , vol.350 , pp. 359-362
    • Guan, K.1    Broyles, S.S.2    Dixon, J.E.3
  • 24
    • 0027509501 scopus 로고
    • Phosphorylation and activation of human cdc25-C by cdc2-cyclin B and its involvement in the self-amplification of MPF at mitosis
    • Hoffmann, I., Clarke, P.R., Marcote, M.J., Karsenti, E., and Draetta, G. (1993). Phosphorylation and activation of human cdc25-C by cdc2-cyclin B and its involvement in the self-amplification of MPF at mitosis. EMBO J. 12, 53-63.
    • (1993) EMBO J. , vol.12 , pp. 53-63
    • Hoffmann, I.1    Clarke, P.R.2    Marcote, M.J.3    Karsenti, E.4    Draetta, G.5
  • 25
    • 0028022034 scopus 로고
    • Activation of the phosphatase activity of human cdc25A by a cdk2-cyclin E dependent phosphorylation at the G1/S transition
    • Hoffmann, I., Draetta, G., and Karsenti, E. (1994). Activation of the phosphatase activity of human cdc25A by a cdk2-cyclin E dependent phosphorylation at the G1/S transition. EMBO J. 13, 4302-4310.
    • (1994) EMBO J. , vol.13 , pp. 4302-4310
    • Hoffmann, I.1    Draetta, G.2    Karsenti, E.3
  • 26
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm, L., and Sander, C. (1994). The FSSP database of structurally aligned protein fold families. Nucleic Acids Res. 22, 3600-3609.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 27
    • 0027339731 scopus 로고
    • Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase
    • Honda, R., Ohba, Y., Nagata, A., Okayama, H., and Yasuda, H. (1993). Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase. FEBS Lett. 318, 331-334.
    • (1993) FEBS Lett. , vol.318 , pp. 331-334
    • Honda, R.1    Ohba, Y.2    Nagata, A.3    Okayama, H.4    Yasuda, H.5
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
    • (1991) Acta Cryst. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 30
    • 0027423987 scopus 로고
    • Amino acid sequence similarity between CL100, a dual-specificity MAP kinase phosphatase and cdc25
    • Keyse, S.M., and Ginsburg, M. (1993). Amino acid sequence similarity between CL100, a dual-specificity MAP kinase phosphatase and cdc25. Trends Biochem. Sci. 18, 377-378.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 377-378
    • Keyse, S.M.1    Ginsburg, M.2
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic figures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic figures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0026006392 scopus 로고
    • Mutations of p34cdc2 phosphorylation sites induce premature mitotic events in HeLa cells: Evidence for a double block to p34cdc2 kinase activation invertebrates
    • Krek, W., and Nigg, E. (1991). Mutations of p34cdc2 phosphorylation sites induce premature mitotic events in HeLa cells: evidence for a double block to p34cdc2 kinase activation invertebrates. EMBO J. 10, 3331-3341.
    • (1991) EMBO J. , vol.10 , pp. 3331-3341
    • Krek, W.1    Nigg, E.2
  • 33
    • 0025980359 scopus 로고
    • The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system
    • Kumagai, A., and Dunphy, W. (1991). The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system. Cell 64, 903-914.
    • (1991) Cell , vol.64 , pp. 903-914
    • Kumagai, A.1    Dunphy, W.2
  • 35
    • 0025845269 scopus 로고
    • Clues to action of cdc25 protein
    • Moreno, S., and Nurse, P. (1991). Clues to action of cdc25 protein. Nature 351, 194.
    • (1991) Nature , vol.351 , pp. 194
    • Moreno, S.1    Nurse, P.2
  • 36
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan, D.O. (1995). Principles of CDK regulation. Nature 374, 131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 37
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter, Jr. and R.M. Sweet, eds. (New York: Academic Press)
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology, Volume 276: Macromolecular Crystallography, part A, C.W. Carter, Jr. and R.M. Sweet, eds. (New York: Academic Press), pp. 307-326.
    • (1997) Methods in Enzymology, Volume 276: Macromolecular Crystallography, Part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216
    • Peng, C.Y., Graves, P.R., Thoma, R.S., Wu, Z., Shaw, A.S., and Piwnica-Worms, H. (1997). Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. Science 277, 1501-1505.
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.Y.1    Graves, P.R.2    Thoma, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 40
    • 0017798493 scopus 로고
    • The covalent and tertiary structure of bovine liver rhodanese
    • Ploegman, J.H., Drent, G., Kalk, K.H., and Hol, W.G. (1978). The covalent and tertiary structure of bovine liver rhodanese. Nature 273, 124-129.
    • (1978) Nature , vol.273 , pp. 124-129
    • Ploegman, J.H.1    Drent, G.2    Kalk, K.H.3    Hol, W.G.4
  • 41
    • 0030833171 scopus 로고    scopus 로고
    • Structure and function of the low M-r phosphotyrosine protein phosphatases
    • Ramponi, G., and Stefani, M. (1997). Structure and function of the low M-r phosphotyrosine protein phosphatases. Biochim. Biophys. Acta 1341, 137-156.
    • (1997) Biochim. Biophys. Acta , vol.1341 , pp. 137-156
    • Ramponi, G.1    Stefani, M.2
  • 42
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., and Sander, C. (1994). Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 43
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo, A., Jeffrey, P., and Pavletich, N. (1996). Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3, 696-700.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.1    Jeffrey, P.2    Pavletich, N.3
  • 44
  • 45
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate
    • Stuckey, J.A., Schubert, H.L., Fauman, E.B., Zhang, Z.-Y., Dixon, J.E., and Saper, M.A. (1994). Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate. Nature 370, 571-575.
    • (1994) Nature , vol.370 , pp. 571-575
    • Stuckey, J.A.1    Schubert, H.L.2    Fauman, E.B.3    Zhang, Z.-Y.4    Dixon, J.E.5    Saper, M.A.6
  • 46
    • 0028030520 scopus 로고
    • The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
    • Su, X.-D., Taddel, N., Stefani, M., Ramponi, G., and Nordlund, P. (1994). The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature 370, 575-579.
    • (1994) Nature , vol.370 , pp. 575-579
    • Su, X.-D.1    Taddel, N.2    Stefani, M.3    Ramponi, G.4    Nordlund, P.5
  • 47
    • 0030728763 scopus 로고    scopus 로고
    • The Saccharomyces cerivisiae ACR3 gene encodes a putative membrane protein involved in transport
    • Wysocki, R., Bobrowicz, P., and Ulaszewski, S. (1997). The Saccharomyces cerivisiae ACR3 gene encodes a putative membrane protein involved in transport. J. Biol. Chem. 272, 30061-30066.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30061-30066
    • Wysocki, R.1    Bobrowicz, P.2    Ulaszewski, S.3
  • 48
    • 0029981395 scopus 로고    scopus 로고
    • Roles of active site residues and the NH2-terminal domain in the catalysis and substrate binding of human Cdc25
    • Xu, X., and Burke, S.P. (1996). Roles of active site residues and the NH2-terminal domain in the catalysis and substrate binding of human Cdc25. J. Biol. Chem. 271, 5118-5124.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5118-5124
    • Xu, X.1    Burke, S.P.2
  • 49
    • 0030970643 scopus 로고    scopus 로고
    • Control of cell cycle progression in human natural killer cells through redox regulation of expression and phosphorylation of retinoblastoma gene product protein
    • Yamauchi, A., and Bloom, E.T. (1997). Control of cell cycle progression in human natural killer cells through redox regulation of expression and phosphorylation of retinoblastoma gene product protein. Blood 89, 4092-4099.
    • (1997) Blood , vol.89 , pp. 4092-4099
    • Yamauchi, A.1    Bloom, E.T.2
  • 50
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual-specificity protein phosphatase VHR
    • Yuvaniyama, J., Denu, J.M., Dixon, J.E., and Saper, M.A. (1996). Crystal structure of the dual-specificity protein phosphatase VHR. Science 272, 1328-1331.
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 51
    • 0028016349 scopus 로고
    • Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-Å resolution
    • Zhang, M., Van Etten, R.L., and Stauffacher, C.V. (1994a). Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-Å resolution. Biochemistry 33, 11097-11105.
    • (1994) Biochemistry , vol.33 , pp. 11097-11105
    • Zhang, M.1    Van Etten, R.L.2    Stauffacher, C.V.3
  • 52
    • 0028176050 scopus 로고
    • Dissecting the catalytic mechanism of protein-tyrosine phosphatases
    • Zhang, Z.-Y., Wang, Y., and Dixon, J.E. (1994b). Dissecting the catalytic mechanism of protein-tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 91, 1624-1627.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1624-1627
    • Zhang, Z.-Y.1    Wang, Y.2    Dixon, J.E.3


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