메뉴 건너뛰기




Volumn 9, Issue 5, 2014, Pages

The Mechanism of allosteric inhibition of protein tyrosine phosphatase 1B

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE 1B; SERINE; TYROSINE; BENZOFURAN; BENZOFURAN DERIVATIVE; PROTEIN BINDING; PTPN1 PROTEIN, HUMAN;

EID: 84901295344     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0097668     Document Type: Article
Times cited : (57)

References (59)
  • 1
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80: 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 2
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter T (2000) Signaling-2000 and beyond. Cell 100: 113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 4
    • 0030296632 scopus 로고    scopus 로고
    • Structure and function of the protein tyrosine phosphatases
    • DOI 10.1016/S0968-0004(96)10059-1, PII S0968000496100591
    • Fauman EB, Saper MA (1996) Structure and function of theprotein tyrosine phosphatases. Trends biochem sci 21: 413-417. (Pubitemid 26393727)
    • (1996) Trends in Biochemical Sciences , vol.21 , Issue.11 , pp. 413-417
    • Fauman, E.B.1    Saper, M.A.2
  • 5
    • 0035415662 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Prospects for therapeutics
    • Zhang ZY (2001) Protein tyrosine phosphatases: prospects for therapeutics. Curr Opin Chem Biol 5: 416-423.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 416-423
    • Zhang, Z.Y.1
  • 6
    • 0034507958 scopus 로고    scopus 로고
    • Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B
    • DOI 10.1016/S1097-2765(00)00137-4
    • Salmeen A, Andersen JN, Myers MP, Tonks NK, Barford D (2000) Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B. Mol cell 6: 1401-1412. (Pubitemid 32045932)
    • (2000) Molecular Cell , vol.6 , Issue.6 , pp. 1401-1412
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Tonks, N.K.4    Barford, D.5
  • 7
    • 84872770077 scopus 로고    scopus 로고
    • PTP1B and TCPTP-nonredundant phosphatases in insulin signaling and glucose homeostasis
    • Tiganis T (2012) PTP1B and TCPTP-nonredundant phosphatases in insulin signaling and glucose homeostasis. FEBS J 280: 445-458.
    • (2012) FEBS J , vol.280 , pp. 445-458
    • Tiganis, T.1
  • 8
    • 34247362854 scopus 로고    scopus 로고
    • PTP1B as a drug target: Recent developments in PTP1B inhibitor discovery
    • DOI 10.1016/j.drudis.2007.03.011, PII S1359644607001365
    • Zhang S, Zhang ZY (2007) PTP1B as a drug target: recent developments in PTP1B inhibitor discovery. Drug Discov Today 12: 373-381. (Pubitemid 46636379)
    • (2007) Drug Discovery Today , vol.12 , Issue.9-10 , pp. 373-381
    • Zhang, S.1    Zhang, Z.-Y.2
  • 9
    • 0037317489 scopus 로고    scopus 로고
    • PTP1B inhibitors as potential therapeutics in the treatment of type 2 diabetes and obesity
    • Zhang ZY, Lee SY (2003) PTP1B inhibitors as potential therapeutics in the treatment of type 2 diabetes and obesity. Expert Opin Investig Drugs 12: 223-233.
    • (2003) Expert Opin Investig Drugs , vol.12 , pp. 223-233
    • Zhang, Z.Y.1    Lee, S.Y.2
  • 12
    • 79955558165 scopus 로고    scopus 로고
    • Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
    • Masterson LR, Shi L, Metcalfe E, Gao J, Taylor SS, et al. (2011) Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy. Proc Natl Acad Sci U S A 108: 6969-6974.
    • (2011) Proc Natl Acad Sci U S a , vol.108 , pp. 6969-6974
    • Masterson, L.R.1    Shi, L.2    Metcalfe, E.3    Gao, J.4    Taylor, S.S.5
  • 13
    • 77958056047 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases as drug targets: Strategies and challenges of inhibitor development
    • Barr AJ (2010) Protein tyrosine phosphatases as drug targets: strategies and challenges of inhibitor development. Future Med Chem 2: 1563-1576.
    • (2010) Future Med Chem , vol.2 , pp. 1563-1576
    • Barr, A.J.1
  • 14
    • 43049126784 scopus 로고    scopus 로고
    • PTP1B and TC-PTP: Regulators of transformation and tumorigenesis
    • Stuible M, Doody KM, Tremblay ML (2008) PTP1B and TC-PTP: regulators of transformation and tumorigenesis. Cancer Metastasis Rev 27: 215-230.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 215-230
    • Stuible, M.1    Doody, K.M.2    Tremblay, M.L.3
  • 15
    • 78651295418 scopus 로고    scopus 로고
    • ASD: A comprehensive database of allosteric proteins and modulators
    • Huang Z, Zhu L, Cao Y, Wu G, Liu X, et al. (2011) ASD: a comprehensive database of allosteric proteins and modulators. Nucleic Acids Res 39: D663-D669.
    • (2011) Nucleic Acids Res , vol.39
    • Huang, Z.1    Zhu, L.2    Cao, Y.3    Wu, G.4    Liu, X.5
  • 16
    • 84891778690 scopus 로고    scopus 로고
    • ASD v2.0: Updated content and novel features focusing on allosteric regulation
    • Huang Z, Mou L, Shen Q, Lu S, Li C, et al. (2014) ASD v2.0: updated content and novel features focusing on allosteric regulation. Nucleic Acids Res 42: D510-D516.
    • (2014) Nucleic Acids Res , vol.42
    • Huang, Z.1    Mou, L.2    Shen, Q.3    Lu, S.4    Li, C.5
  • 17
    • 84865515439 scopus 로고    scopus 로고
    • Molecular Dynamics Approach to Probe the Allosteric Inhibition of PTP1B by Chlorogenic and Cichoric Acid
    • Baskaran SK, Goswami N, Selvaraj S, Muthusamy VS, Lakshmi BS, et al. (2012) Molecular Dynamics Approach to Probe the Allosteric Inhibition of PTP1B by Chlorogenic and Cichoric Acid. J Chem Inf Model 52: 2004-2012.
    • (2012) J Chem Inf Model , vol.52 , pp. 2004-2012
    • Baskaran, S.K.1    Goswami, N.2    Selvaraj, S.3    Muthusamy, V.S.4    Lakshmi, B.S.5
  • 19
    • 0034635121 scopus 로고    scopus 로고
    • Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia
    • DOI 10.1021/bi991570i
    • Hoff RH, Hengge AC, Wu L, Keng YF, Zhang ZY, et al. (2000) Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia. Biochemistry 39: 46-54. (Pubitemid 30033318)
    • (2000) Biochemistry , vol.39 , Issue.1 , pp. 46-54
    • Hoff, R.H.1    Hengge, A.C.2    Wu, L.3    Keng, Y.-F.4    Zhang, Z.-Y.5
  • 20
    • 34047252001 scopus 로고    scopus 로고
    • The role of the C-terminal domain of protein tyrosine phosphatase-1B in phosphatase activity and substrate binding
    • DOI 10.1074/jbc.M610096200
    • Picha KM, Patel SS, Mandiyan S, Koehn J, Wennogle LP, et al. (2007) The role of the C-terminal domain of protein tyrosine phosphatase-1B in phosphatase activity and substrate binding. J Biol Chem 282: 2911-2917. (Pubitemid 47084320)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.5 , pp. 2911-2917
    • Picha, K.M.1    Patel, S.S.2    Mandiyan, S.3    Koehn, J.4    Wennogle, L.P.5
  • 23
    • 77954052098 scopus 로고    scopus 로고
    • Probing interaction requirements in PTP1B inhibitors: A comparative molecular dynamics study
    • Kumar R, Shinde RN, Ajay D, Sobhia ME (2010) Probing interaction requirements in PTP1B inhibitors: a comparative molecular dynamics study. J Chem Inf Model 50: 1147-1158.
    • (2010) J Chem Inf Model , vol.50 , pp. 1147-1158
    • Kumar, R.1    Shinde, R.N.2    Ajay, D.3    Sobhia, M.E.4
  • 24
    • 79952228322 scopus 로고    scopus 로고
    • Alpha7 helix plays an important role in the conformational stability of PTP1B
    • Olmez EO, Alakent B (2011) Alpha7 helix plays an important role in the conformational stability of PTP1B. J Biomol Struct Dyn 28: 675-693.
    • (2011) J Biomol Struct Dyn , vol.28 , pp. 675-693
    • Olmez, E.O.1    Alakent, B.2
  • 25
    • 84878167933 scopus 로고    scopus 로고
    • Unraveling the allosteric inhibition mechanism of PTP1B by free energy calculation based on umbrella sampling
    • Cui W, Cheng Y, Geng L, Liang D, Hou T, et al. (2013) Unraveling the allosteric inhibition mechanism of PTP1B by free energy calculation based on umbrella sampling. J Chem Inf Model 53: 1157-1167.
    • (2013) J Chem Inf Model , vol.53 , pp. 1157-1167
    • Cui, W.1    Cheng, Y.2    Geng, L.3    Liang, D.4    Hou, T.5
  • 28
    • 0031457541 scopus 로고    scopus 로고
    • Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design
    • Puius YA, Zhao Y, Sullivan M, Lawrence DS, Almo SC, et al. (1997) Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design. Proc Natl Acad Sci U S A 94: 13420-13425.
    • (1997) Proc Natl Acad Sci U S a , vol.94 , pp. 13420-13425
    • Puius, Y.A.1    Zhao, Y.2    Sullivan, M.3    Lawrence, D.S.4    Almo, S.C.5
  • 29
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford D, Flint AJ, Tonks NK (1994) Crystal structure of human protein tyrosine phosphatase 1B. Science 263: 1397-1404. (Pubitemid 24137822)
    • (1994) Science , vol.263 , Issue.5152 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 30
    • 84901380246 scopus 로고    scopus 로고
    • Version S 6.8 (2001) Tripos Associates Inc. St. Louis, MO
    • Version S 6.8 (2001) Tripos Associates Inc. St. Louis, MO.
  • 33
    • 0030887994 scopus 로고    scopus 로고
    • Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1
    • DOI 10.1021/bi963094r
    • Lohse DL, Denu JM, Santoro N, Dixon JE (1997) Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1. Biochemistry 36: 4568-4575. (Pubitemid 27180305)
    • (1997) Biochemistry , vol.36 , Issue.15 , pp. 4568-4575
    • Lohse, D.L.1    Denu, J.M.2    Santoro, N.3    Dixon, J.E.4
  • 34
    • 0032976539 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein-tyrosine phosphatase 1B. I. Ligand-induced changes in the protein motions
    • Peters GH, Frimurer TM, Andersen JN, Olsen OH (1999) Molecular dynamics simulations of protein-tyrosine phosphatase 1B. I. Ligand-induced changes in the protein motions. Biophys J 77: 505-515. (Pubitemid 29305246)
    • (1999) Biophysical Journal , vol.77 , Issue.1 , pp. 505-515
    • Peters, G.H.1    Frimurer, T.M.2    Andersen, J.N.3    Olsen, O.H.4
  • 35
    • 0034026757 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein-tyrosine phosphatase 1B. II. Substrate-enzyme interactions and dynamics
    • Peters GH, Frimurer TM, Andersen JN, Olsen OH (2000) Molecular dynamics simulations of protein-tyrosine phosphatase 1B. II. Substrate-enzyme interactions and dynamics. Biophys J 78: 2191-2200. (Pubitemid 30313782)
    • (2000) Biophysical Journal , vol.78 , Issue.5 , pp. 2191-2200
    • Peters, G.H.1    Frimurer, T.M.2    Andersen, J.N.3    Olsen, O.H.4
  • 36
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan Y, Wu C, Chowdhury S, Lee MC, Xiong G, et al. (2003) A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J Comput Chem 24: 1999-2012.
    • (2003) J Comput Chem , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5
  • 38
    • 79960279272 scopus 로고    scopus 로고
    • Molecular modeling and molecular dynamics simulation studies of the GSK3b/ATP/substrate complex: Understanding the unique P+4 primed phosphorylation specificity for GSK3b substrates
    • Lu S, Jiang Y, Zou J, Wu T (2011) Molecular modeling and molecular dynamics simulation studies of the GSK3b/ATP/substrate complex: understanding the unique P+4 primed phosphorylation specificity for GSK3b substrates. J Chem Inf Model 51: 1025-1036.
    • (2011) J Chem Inf Model , vol.51 , pp. 1025-1036
    • Lu, S.1    Jiang, Y.2    Zou, J.3    Wu, T.4
  • 39
    • 84866709839 scopus 로고    scopus 로고
    • Insights into the role of magnesium triad in myo-inositol monophosphatase: Metal mechanism, substrate binding, and lithium therapy
    • Lu S, Huang W, Li X, Huang Z, Liu X, et al. (2012) Insights into the role of magnesium triad in myo-inositol monophosphatase: metal mechanism, substrate binding, and lithium therapy. J Chem Inf Model 52: 2398-2409.
    • (2012) J Chem Inf Model , vol.52 , pp. 2398-2409
    • Lu, S.1    Huang, W.2    Li, X.3    Huang, Z.4    Liu, X.5
  • 40
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N· log (N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An N· log (N) method for Ewald sums in large systems. J Chem Phys 98: 10089.
    • (1993) J Chem Phys , vol.98 , pp. 10089
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 41
    • 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 HJ (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Chem Phys 23: 327-341.
    • (1977) J Chem Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.3
  • 42
    • 0242509772 scopus 로고    scopus 로고
    • Self-guided Langevin dynamics simulation method
    • Wu X, Brooks BR (2003) Self-guided Langevin dynamics simulation method. Chem Phys Lett 381: 512-518.
    • (2003) Chem Phys Lett , vol.381 , pp. 512-518
    • Wu, X.1    Brooks, B.R.2
  • 47
    • 34147158317 scopus 로고    scopus 로고
    • Loop dynamics and ligand binding kinetics in the reaction catalyzed by the Yersinia protein tyrosine phosphatase
    • DOI 10.1021/bi602335x
    • Khajehpour M, Wu L, Liu S, Zhadin N, Zhang ZY, et al. (2007) Loop dynamics and ligand binding kinetics in the reaction catalyzed by the Yersinia protein tyrosine phosphatase. Biochemistry 46: 4370-4378. (Pubitemid 46559402)
    • (2007) Biochemistry , vol.46 , Issue.14 , pp. 4370-4378
    • Khajehpour, M.1    Wu, L.2    Liu, S.3    Zhadin, N.4    Zhang, Z.-Y.5    Callender, R.6
  • 48
    • 0031043155 scopus 로고    scopus 로고
    • Rapid loop dynamics of yersinia protein tyrosine phosphatases
    • DOI 10.1021/bi9622130
    • Juszczak LJ, Zhang ZY, Wu L, Gottfried DS, Eads DD (1997) Rapid loop dynamics of Yersinia protein tyrosine phosphatases. Biochemistry 36: 2227-2236. (Pubitemid 27104716)
    • (1997) Biochemistry , vol.36 , Issue.8 , pp. 2227-2236
    • Juszczak, L.J.1    Zhang, Z.-Y.2    Wu, L.3    Gottfried, D.S.4    Eads, D.D.5
  • 49
    • 0032500638 scopus 로고    scopus 로고
    • Molecular basis for substrate specificity of protein-tyrosine phosphatase 1B
    • DOI 10.1074/jbc.273.41.26368
    • Sarmiento M, Zhao Y, Gordon SJ, Zhang ZY (1998) Molecular basis for substrate specificity of protein-tyrosine phosphatase 1B. The J Biol Chem 273: 26368-74. (Pubitemid 28471640)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26368-26374
    • Sarmiento, M.1    Zhao, Y.2    Gordon, S.J.3    Zhang, Z.-Y.4
  • 50
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
    • Jia Z, Barford D, Flint AJ, Tonks NK (1995) Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 268: 1754-1758.
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks, N.K.4
  • 51
    • 12144290569 scopus 로고    scopus 로고
    • Residue 182 influences the second step of protein-tyrosine phosphatase-mediated catalysis
    • Pedersen A, GUO X, MLLER K, Peters G, Andersen H, et al. (2004) Residue 182 influences the second step of protein-tyrosine phosphatase-mediated catalysis. Biochem J 378: 421-433.
    • (2004) Biochem J , vol.378 , pp. 421-433
    • Pedersen, A.1    Guo, X.2    Mller, K.3    Peters, G.4    Andersen, H.5
  • 52
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 257722637.
    • (1983) Biopolymers , vol.22 , pp. 257722637
    • Kabsch, W.1    Sander, C.2
  • 53
    • 84883468084 scopus 로고    scopus 로고
    • Allosite: A method for predicting allosteric sites
    • Huang W, Lu S, Huang Z, Liu X, Mou L, et al. (2013) Allosite: a method for predicting allosteric sites. Bioinformatics 29: 2357-2359.
    • (2013) Bioinformatics , vol.29 , pp. 2357-2359
    • Huang, W.1    Lu, S.2    Huang, Z.3    Liu, X.4    Mou, L.5
  • 55
    • 84872394356 scopus 로고    scopus 로고
    • Towards an understanding of the sequence and structural basis of allosteric proteins
    • Li X, Chen Y, Lu S, Huang Z, Liu X, et al. (2013) Towards an understanding of the sequence and structural basis of allosteric proteins. J Mol Graph Model 40: 30-39.
    • (2013) J Mol Graph Model , vol.40 , pp. 30-39
    • Li, X.1    Chen, Y.2    Lu, S.3    Huang, Z.4    Liu, X.5
  • 56
    • 67651083215 scopus 로고    scopus 로고
    • Lys169 of human glucokinase is a determinant for glucose phosphorylation: Implication for the atomic mechanism of glucokinase catalysis
    • Zhang J, Li C, Shi T, Chen K, Shen X, et al. (2009) Lys169 of human glucokinase is a determinant for glucose phosphorylation: implication for the atomic mechanism of glucokinase catalysis. PLoS One 4: e6304.
    • (2009) PLoS One , vol.4
    • Zhang, J.1    Li, C.2    Shi, T.3    Chen, K.4    Shen, X.5
  • 57
    • 84867485710 scopus 로고    scopus 로고
    • Toward understanding the molecular basis for chemical allosteric modulator design
    • Wang Q, Zheng M, Huang Z, Liu X, Zhou H, et al. (2012) Toward understanding the molecular basis for chemical allosteric modulator design. J Mol Graph Model 38: 324-333.
    • (2012) J Mol Graph Model , vol.38 , pp. 324-333
    • Wang, Q.1    Zheng, M.2    Huang, Z.3    Liu, X.4    Zhou, H.5
  • 58
    • 82355168473 scopus 로고    scopus 로고
    • Computational screening for active compounds targeting protein sequences: Methodology and experimental validation
    • Wang F, Liu D, Wang H, Luo C, Zheng M, et al. (2011) Computational screening for active compounds targeting protein sequences: methodology and experimental validation. J Chem Inf Model 51: 2821-2828.
    • (2011) J Chem Inf Model , vol.51 , pp. 2821-2828
    • Wang, F.1    Liu, D.2    Wang, H.3    Luo, C.4    Zheng, M.5
  • 59
    • 84907979005 scopus 로고    scopus 로고
    • Harnessing allostery: A novel approach to drug discovery
    • doi:10.1002/med.21317
    • Lu S, Li S, Zhang J (2014) Harnessing allostery: a novel approach to drug discovery. Med Res Rev doi:10.1002/med.21317.
    • (2014) Med Res Rev
    • Lu, S.1    Li, S.2    Zhang, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.