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Volumn 15, Issue 24, 1996, Pages 6798-6809

Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 Å resolution

Author keywords

Catalytic mechanism; Metalloenzyme; Protein phosphatase 2C; Signal transduction; X ray crystallography

Indexed keywords

ADENYLATE CYCLASE; MAGNESIUM ION; MANGANESE; PHOSPHOPROTEIN PHOSPHATASE; PYRUVATE DEHYDROGENASE PHOSPHATASE;

EID: 0030465532     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb01071.x     Document Type: Article
Times cited : (402)

References (57)
  • 1
    • 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
  • 2
    • 0028880718 scopus 로고
    • Protein tyrosine phosphatases take off
    • Barford,D., Jia,Z. and Tonks,N.K. (1995) Protein tyrosine phosphatases take off. Nature Struct. Biol., 2, 1043-1053.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1043-1053
    • Barford, D.1    Jia, Z.2    Tonks, N.K.3
  • 3
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton,G.J. (1993) ALSCRIPT: a tool to format multiple sequence alignments. Protein Engng, 6, 37-40.
    • (1993) Protein Engng , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 4
    • 0023518540 scopus 로고
    • A strategy for the rapid multiple alignment of protein sequences
    • Barton,G.J. and Sternberg,M.J.E. (1987) A strategy for the rapid multiple alignment of protein sequences. J. Mol. Biol., 198, 327-337.
    • (1987) J. Mol. Biol. , vol.198 , pp. 327-337
    • Barton, G.J.1    Sternberg, M.J.E.2
  • 5
    • 0029954661 scopus 로고    scopus 로고
    • The protein phosphatase 2C (PP2C) superfamily: Detection of bacterial homologues
    • Bork,P., Brown,N.P., Hegyi,H. and Shultz,J. (1996) The protein phosphatase 2C (PP2C) superfamily: detection of bacterial homologues. Protein Sci., 5, 1421-1425.
    • (1996) Protein Sci. , vol.5 , pp. 1421-1425
    • Bork, P.1    Brown, N.P.2    Hegyi, H.3    Shultz, J.4
  • 6
    • 0027522757 scopus 로고
    • PPX, a novel protein serine/threonine phosphatase localised to centrosomes
    • Brewis,N.D., Street,A.J., Prescott,A.R. and Cohen,P.T.W. (1993) PPX, a novel protein serine/threonine phosphatase localised to centrosomes. EMBO J., 12, 987-996..
    • (1993) EMBO J. , vol.12 , pp. 987-996
    • Brewis, N.D.1    Street, A.J.2    Prescott, A.R.3    Cohen, P.T.W.4
  • 8
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen,P. (1989) The structure and regulation of protein phosphatases. Annu. Rev. Biochem., 58, 453-508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 9
    • 0001574833 scopus 로고
    • Nomenclature and chromosomal localisation of human protein serine/threonine phosphatase gene
    • Cohen,P.T.W. (1994) Nomenclature and chromosomal localisation of human protein serine/threonine phosphatase gene. Adv. Protein Phosphat., 8, 371-376.
    • (1994) Adv. Protein Phosphat. , vol.8 , pp. 371-376
    • Cohen, P.T.W.1
  • 10
    • 0025352668 scopus 로고
    • Mutational mapping of ras-responsive domains of the Saccharomyces cerevisiae adenylyl cyclase
    • Coliccelli,J., Field,J., Ballester,R., Chester,N., Young,D. and Wigler,M. (1990) Mutational mapping of ras-responsive domains of the Saccharomyces cerevisiae adenylyl cyclase. Mol. Cell. Biol., 10, 2539-2543.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2539-2543
    • Coliccelli, J.1    Field, J.2    Ballester, R.3    Chester, N.4    Young, D.5    Wigler, M.6
  • 11
    • 0029561919 scopus 로고
    • 5′-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase 2Cα and PP2AC
    • Davies,S.P., Helps,N.R., Cohen,P.T.W. and Hardie,D.G. (1995) 5′-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase 2Cα and PP2AC. FEBS Lett., 377, 421-425.
    • (1995) FEBS Lett. , vol.377 , pp. 421-425
    • Davies, S.P.1    Helps, N.R.2    Cohen, P.T.W.3    Hardie, D.G.4
  • 12
    • 0025157179 scopus 로고
    • An investigation of the substrate specificity to protein phosphatase 2C using synthetic peptide substrates. Comparison with protein phosphatase 2A
    • Donella Deana,A., McGowan,C.H., Cohen,P., Marciori,R, Meyer,H.E. and Pinna,L.A. (1990) An investigation of the substrate specificity to protein phosphatase 2C using synthetic peptide substrates. Comparison with protein phosphatase 2A. Biochim. Biophys. Acta, 1051, 199-202.
    • (1990) Biochim. Biophys. Acta , vol.1051 , pp. 199-202
    • Donella Deana, A.1    McGowan, C.H.2    Cohen, P.3    Marciori, R.4    Meyer, H.E.5    Pinna, L.A.6
  • 13
    • 0028788997 scopus 로고
    • Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division
    • Duncan,L., Alper,S., Arigoni,F., Losick,R. and Stragier,P. (1995) Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division. Science, 270, 641-644.
    • (1995) Science , vol.270 , pp. 641-644
    • Duncan, L.1    Alper, S.2    Arigoni, F.3    Losick, R.4    Stragier, P.5
  • 14
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase I and its complex with tungstate
    • Egloff,M.-P., Cohen,P.T.W., Reinemer,P. and Barford,D. (1995) Crystal structure of the catalytic subunit of human protein phosphatase I and its complex with tungstate. J. Mol. Biol., 254, 942-959.
    • (1995) J. Mol. Biol. , vol.254 , pp. 942-959
    • Egloff, M.-P.1    Cohen, P.T.W.2    Reinemer, P.3    Barford, D.4
  • 15
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three dimensional solid model representation of macromolecules
    • Evans,S.V. (1993) SETOR: hardware lighted three dimensional solid model representation of macromolecules. J. Mol. Graphics, 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 17
    • 0002701928 scopus 로고
    • PHASES - A program package for the processing and analysis of diffraction data from macromolecules
    • Furey,W. and Swaminathan,S. (1990) PHASES - a program package for the processing and analysis of diffraction data from macromolecules. Am. Cryst. Assoc. Meeting Summ., 18, 73.
    • (1990) Am. Cryst. Assoc. Meeting Summ. , vol.18 , pp. 73
    • Furey, W.1    Swaminathan, S.2
  • 18
    • 0029094754 scopus 로고
    • Three dimensional structure of the catalytic subunit of protein serine/threonine phosphalase-1
    • Goldberg,J., Huang,H., Kwon,Y., Greengard,P., Nairn,A.C. and Kuriyan,J. (1995) Three dimensional structure of the catalytic subunit of protein serine/threonine phosphalase-1. Nature, 376, 745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.2    Kwon, Y.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 19
    • 0029133116 scopus 로고
    • X-ray structure of calcineurin inhibited by the iinmunophilin-immunosuppressant FKBP12-FK506 complex
    • Griffith,J.P. et al. (1995) X-ray structure of calcineurin inhibited by the iinmunophilin-immunosuppressant FKBP12-FK506 complex. Cell, 82, 507-522.
    • (1995) Cell , vol.82 , pp. 507-522
    • Griffith, J.P.1
  • 21
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson,W.A., Horton,J.R. and LeMaster,D.M. (1990) Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J., 9, 1665-1758.
    • (1990) EMBO J. , vol.9 , pp. 1665-1758
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 22
    • 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 Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
    • 0022379619 scopus 로고
    • DNA sequence and characterization of the S. cerevisiae gene encoding adenylate cyclase
    • Kataoka,T., Broek,D. and Wigler,M. (1985) DNA sequence and characterization of the S. cerevisiae gene encoding adenylate cyclase. Cell, 43, 493-505.
    • (1985) Cell , vol.43 , pp. 493-505
    • Kataoka, T.1    Broek, D.2    Wigler, M.3
  • 24
    • 0027279242 scopus 로고
    • Protein phosphatase 1, 2A, and 2C are protein histidine phosphatases
    • Kim,Y., Huang,J., Cohen,P. and Matthews,H.R. (1993) Protein phosphatase 1, 2A, and 2C are protein histidine phosphatases. J. Biol. Chem., 268, 18513-18518.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18513-18518
    • Kim, Y.1    Huang, J.2    Cohen, P.3    Matthews, H.R.4
  • 25
    • 0028848524 scopus 로고
    • Crystal structure of human calcineurin and the human FKBP12-FK506-calcineurin complex
    • Kissinger,C.R. et al. (1995) Crystal structure of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature, 378, 641-644.
    • (1995) Nature , vol.378 , pp. 641-644
    • Kissinger, C.R.1
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis,P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 29
    • 0027861114 scopus 로고
    • Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C
    • Lawson,J.E., Niu,X.-D., Browning,K.S., Trong,H.L., Yan,J. and Reed,L.J. (1993) Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C. Biochemistry, 32, 8987-8993.
    • (1993) Biochemistry , vol.32 , pp. 8987-8993
    • Lawson, J.E.1    Niu, X.-D.2    Browning, K.S.3    Trong, H.L.4    Yan, J.5    Reed, L.J.6
  • 30
    • 0028339956 scopus 로고
    • Arabidopsis ABA response gene ABII: Features of a calcium-modulated protein phosphatase
    • Leung,J., Bouvier-Durand,M., Morris,P.-C., Guerrier,D., Chefdor,F. and Giraudat,J. (1994) Arabidopsis ABA response gene ABII: features of a calcium-modulated protein phosphatase. Science, 264, 1448-1452.
    • (1994) Science , vol.264 , pp. 1448-1452
    • Leung, J.1    Bouvier-Durand, M.2    Morris, P.-C.3    Guerrier, D.4    Chefdor, F.5    Giraudat, J.6
  • 31
    • 0027764344 scopus 로고
    • Protein sequence alignments: A strategy for hierarchical analysis of residue conservation
    • Livingston,C.D. and Barton,G.J. (1993) Protein sequence alignments: a strategy for hierarchical analysis of residue conservation. Comput. Applic. Biosci., 9, 745-756.
    • (1993) Comput. Applic. Biosci. , vol.9 , pp. 745-756
    • Livingston, C.D.1    Barton, G.J.2
  • 32
    • 0028228109 scopus 로고
    • A two-component system that regulates an osmosensing MAP kinase cascade in yeast
    • Maeda,T., Wurgler-Murphy,S.M. and Saito,H. (1994) A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature, 369, 242-245.
    • (1994) Nature , vol.369 , pp. 242-245
    • Maeda, T.1    Wurgler-Murphy, S.M.2    Saito, H.3
  • 33
    • 0026547155 scopus 로고
    • Mammalian protein serine/threonine phosphatase 2C: CDNA cloning and comparative analysis of amino acid sequence
    • Mann,D.J., Campbell,D.G., McGowan,C.H. and Cohen,P.T.W.C. (1992) Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequence. Biochim. Biophys. Acta. 1130, 100-104.
    • (1992) Biochim. Biophys. Acta. , vol.1130 , pp. 100-104
    • Mann, D.J.1    Campbell, D.G.2    McGowan, C.H.3    Cohen, P.T.W.C.4
  • 34
    • 0028337360 scopus 로고
    • Isotope effects on the mechanism of calcineurin catalysis: Kinetic solvent isotope and isotope exchange studies
    • Martin,B.L. and Graves,D.J. (1994) Isotope effects on the mechanism of calcineurin catalysis: kinetic solvent isotope and isotope exchange studies. Biochim. Biophys. Acta, 1206, 136-142.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 136-142
    • Martin, B.L.1    Graves, D.J.2
  • 35
    • 0028233382 scopus 로고
    • A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana
    • Meyer,K., Leube,M.P. and Grill,E. (1994) A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana. Science, 264, 1452-1455.
    • (1994) Science , vol.264 , pp. 1452-1455
    • Meyer, K.1    Leube, M.P.2    Grill, E.3
  • 36
    • 0028101461 scopus 로고
    • Quantitative analysis of mutually competitive binding of human raf-1 and yeast adenylyl cyclase to ras proteins
    • Minato,T., Wang,J., Akasaka,K., Okada,T., Suzuki,N. and Kataoka,T. (1994) Quantitative analysis of mutually competitive binding of human raf-1 and yeast adenylyl cyclase to ras proteins. J. Biol. Chem., 269, 20845-20851.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20845-20851
    • Minato, T.1    Wang, J.2    Akasaka, K.3    Okada, T.4    Suzuki, N.5    Kataoka, T.6
  • 37
    • 0028923440 scopus 로고    scopus 로고
    • Structure and function of the multi functional DNA-repair enzyme exonuclease III
    • Moi,C.D., Kuo,C.-F., Thayer,M.M., Cunnigham,R.P. and Tainer,J.A. (1996) Structure and function of the multi functional DNA-repair enzyme exonuclease III. Nature, 374, 381-386.
    • (1996) Nature , vol.374 , pp. 381-386
    • Moi, C.D.1    Kuo, C.-F.2    Thayer, M.M.3    Cunnigham, R.P.4    Tainer, J.A.5
  • 38
    • 0025915269 scopus 로고
    • Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP-activated protein kinase
    • Moore,F., Weekes,J. and Hardie,D.G. (1991) Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP-activated protein kinase. Eur. J. Biochem., 199, 691-697.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 691-697
    • Moore, F.1    Weekes, J.2    Hardie, D.G.3
  • 39
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilising successive over relaxation to solve the Poisson-Boltzmann equation
    • Nicholls,A. and Honig,B. (1991) A rapid finite difference algorithm, utilising successive over relaxation to solve the Poisson-Boltzmann equation. J. Comput. Chem., 12, 435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 40
    • 0002452464 scopus 로고
    • DENZO
    • Sawyer,L., Isaacs,N. and Bailey,S. (eds), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski,Z. (1993) DENZO. In Sawyer,L., Isaacs,N. and Bailey,S. (eds), Data Collection and Processing. SERC Daresbury Laboratory, Warrington, UK, p. 56.
    • (1993) Data Collection and Processing , pp. 56
    • Otwinowski, Z.1
  • 41
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
    • Pai,E.F., Kabsch,W., Krengel,U., Holmes,K.C., John,J. and Wittinghofer,A. (1989) Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature, 341, 209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 42
    • 0026100262 scopus 로고
    • Regulation of smooth muscle phosphatase-II by divalent cations
    • Pato,M.D. and Kerc,E. (1991) Regulation of smooth muscle phosphatase-II by divalent cations. Mol. Cell. Biochem., 101, 31-41.
    • (1991) Mol. Cell. Biochem. , vol.101 , pp. 31-41
    • Pato, M.D.1    Kerc, E.2
  • 43
    • 0028224707 scopus 로고
    • TPDI of Saccharomyces cerevisiae encodes a protein phosphatase 2C-like activity implicated in tRNA splicing and cell separation
    • Robinson,M.K., van Zyl,W.H., Phizicky,E.M. and Broach,J.R. (1994) TPDI of Saccharomyces cerevisiae encodes a protein phosphatase 2C-like activity implicated in tRNA splicing and cell separation. Mol. Cell. Biol., 14, 3634-3645.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3634-3645
    • Robinson, M.K.1    Van Zyl, W.H.2    Phizicky, E.M.3    Broach, J.R.4
  • 44
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases - New avenues for cell regulation
    • Shenolikar,S. (1994) Protein serine/threonine phosphatases - new avenues for cell regulation. Annu. Rev. Cell. Biol., 10, 56-86.
    • (1994) Annu. Rev. Cell. Biol. , vol.10 , pp. 56-86
    • Shenolikar, S.1
  • 45
    • 0028855423 scopus 로고
    • Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase kinase homolog in the osmoregulation of fission yeast
    • Shiozaki,K. and Russell,P. (1995) Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase kinase homolog in the osmoregulation of fission yeast. EMBO J., 14, 492-502.
    • (1995) EMBO J. , vol.14 , pp. 492-502
    • Shiozaki, K.1    Russell, P.2
  • 46
    • 0028298227 scopus 로고
    • Protein phosphatase 2C, encoded by ptcl+, is important in the heat shock response of Schizosaccharomyces pombe
    • Shiozaki,K., Akhavan-Niaki,H., McGowan,C.H. and Russell,P. (1994) Protein phosphatase 2C, encoded by ptcl+, is important in the heat shock response of Schizosaccharomyces pombe. Mol. Cell. Biol., 14, 3742-3751.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3742-3751
    • Shiozaki, K.1    Akhavan-Niaki, H.2    McGowan, C.H.3    Russell, P.4
  • 47
    • 0028075896 scopus 로고
    • Interaction of protein phosphatase with an Arabidopsis serinethreonine receptor kinase
    • Stone,J.M., Collinge,M.A., Smith,R.D., Horn,M.A. and Walker,J.C. (1994) Interaction of protein phosphatase with an Arabidopsis serinethreonine receptor kinase. Science, 266, 793-795.
    • (1994) Science , vol.266 , pp. 793-795
    • Stone, J.M.1    Collinge, M.A.2    Smith, R.D.3    Horn, M.A.4    Walker, J.C.5
  • 48
    • 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
  • 49
    • 0028030520 scopus 로고
    • The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
    • Su,X.-D., Taddei,N., Stefani,M., Ramponi,G. and Nordlund,P. (1994) The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature, 370, 575-578.
    • (1994) Nature , vol.370 , pp. 575-578
    • Su, X.-D.1    Taddei, N.2    Stefani, M.3    Ramponi, G.4    Nordlund, P.5
  • 50
    • 0021511076 scopus 로고
    • Three dimensional structure of bovine pancreatic DNase I at 2.5 Å resolution
    • Suck,D., Oefner,C. and Kabsch,W. (1984) Three dimensional structure of bovine pancreatic DNase I at 2.5 Å resolution. EMBO J., 3, 2423-2430.
    • (1984) EMBO J. , vol.3 , pp. 2423-2430
    • Suck, D.1    Oefner, C.2    Kabsch, W.3
  • 53
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera,S. and Hemmings,B.A. (1995) Serine/threonine protein phosphatases. Kochern. J., 311, 17-29.
    • (1995) Kochern. J. , vol.311 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 54
    • 0028859016 scopus 로고
    • Four additional genes in the sigB operon of Bacillus subtilis that control activity of the general stress factor sB in response to environmental signals
    • Wise,A.A. and Price,C.W. (1995) Four additional genes in the sigB operon of Bacillus subtilis that control activity of the general stress factor sB in response to environmental signals. J. Bacteriol., 177, 123-133.
    • (1995) J. Bacteriol. , vol.177 , pp. 123-133
    • Wise, A.A.1    Price, C.W.2
  • 55
    • 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. (1994) 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
  • 56
    • 0028155865 scopus 로고
    • Protein tyrosine phosphatases: Mechanism of catalysis and substrate specificity
    • Zhang,Z.Y. and Dixon,J.E. (1994) Protein tyrosine phosphatases: mechanism of catalysis and substrate specificity. Adv. Enzymol. Relat. Areas Mol. Biol. 68, 1-38.
    • (1994) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.68 , pp. 1-38
    • Zhang, Z.Y.1    Dixon, J.E.2
  • 57


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