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Volumn 11, Issue 8, 2004, Pages 730-737

Allosteric inhibition of protein tyrosine phosphatase 1B

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; INSULIN; PROTEIN TYROSINE PHOSPHATASE 1B;

EID: 3543017313     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb803     Document Type: Article
Times cited : (463)

References (40)
  • 1
    • 0035936763 scopus 로고    scopus 로고
    • New perspectives into the molecular pathogenesis and treatment of type 2 diabetes
    • Saltiel, A.R. New perspectives into the molecular pathogenesis and treatment of type 2 diabetes. Cell 104, 517-529 (2001).
    • (2001) Cell , vol.104 , pp. 517-529
    • Saltiel, A.R.1
  • 2
    • 0029130199 scopus 로고
    • Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway
    • Ahmad, F., Li, P.M., Meyerovitch, J. & Goldstein, B.J. Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway. J. Biol. Chem. 270, 20503-20508 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 20503-20508
    • Ahmad, F.1    Li, P.M.2    Meyerovitch, J.3    Goldstein, B.J.4
  • 3
    • 0029762957 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B interacts with the activated insulin receptor
    • Seely, B.L. et al. Protein tyrosine phosphatase 1B interacts with the activated insulin receptor. Diabetes 45, 1379-1385 (1996).
    • (1996) Diabetes , vol.45 , pp. 1379-1385
    • Seely, B.L.1
  • 4
    • 0029810614 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling
    • Kenner, K.A., Anyanwu, E., Olefsky, J.M. & Kusari, J. Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling. J. Biol. Chem. 271, 19810-19816 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 19810-19816
    • Kenner, K.A.1    Anyanwu, E.2    Olefsky, J.M.3    Kusari, J.4
  • 5
    • 0030961536 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases PTP1B and syp are modulators of insulin-stimulated translocation of GLUT4 in transfected rat adipose cells
    • Chen, H. et al. Protein-tyrosine phosphatases PTP1B and syp are modulators of insulin-stimulated translocation of GLUT4 in transfected rat adipose cells. J. Biol. Chem. 272, 8026-8031 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 8026-8031
    • Chen, H.1
  • 6
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • Elchebly, M. et al. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 283, 1544-1548 (1999).
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1
  • 7
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • Klaman, L.D. et al. Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell. Biol. 20, 5479-5489 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5479-5489
    • Klaman, L.D.1
  • 8
    • 0036329620 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B reduction regulates adiposity and expression of genes involved in lipogenesis
    • Rondinone, C.M. et al. Protein tyrosine phosphatase 1B reduction regulates adiposity and expression of genes involved in lipogenesis. Diabetes 51, 2405-2411 (2002).
    • (2002) Diabetes , vol.51 , pp. 2405-2411
    • Rondinone, C.M.1
  • 9
    • 0037143754 scopus 로고    scopus 로고
    • PTP1B antisense oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitivity in diabetic mice
    • Zinker, B.A. et al. PTP1B antisense oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitivity in diabetic mice. Proc. Natl. Acad. Sci. USA 99, 11357-11362 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11357-11362
    • Zinker, B.A.1
  • 11
    • 13044270997 scopus 로고    scopus 로고
    • PTP1B inhibition and antihyperglycemic activity in the ob/ob mouse model of novel 11-arylbenzo[b]naphtho[2,3-d]furans and 11-arylbenzo[b]naphtho[2,3-d] thiophenes
    • Wrobel, J. et al. PTP1B inhibition and antihyperglycemic activity in the ob/ob mouse model of novel 11-arylbenzo[b]naphtho[2,3-d]furans and 11-arylbenzo[b]naphtho[2,3-d]thiophenes. J. Med. Chem. 42, 3199-3202 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 3199-3202
    • Wrobel, J.1
  • 12
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford, D., Flint, A.J. & Tonks, N.K. Crystal structure of human protein tyrosine phosphatase 1B. Science 263, 1397-1404 (1994).
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 13
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
    • Jia, Z., Barford, D., Flint, A.J. & Tonks, N.K. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 268, 1754-1758 (1995).
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks, N.K.4
  • 14
    • 0031457541 scopus 로고    scopus 로고
    • Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design
    • Puius, Y.A. et al. Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design. Proc. Natl. Acad. Sci. USA 94, 13420-13425 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13420-13425
    • Puius, Y.A.1
  • 15
    • 0034615991 scopus 로고    scopus 로고
    • Structure-based design of a low molecular weight, nonphosphorus, nonpeptide, and highly selective inhibitor of protein-tyrosine phosphatase 1B
    • Iversen, L.F. et al. Structure-based design of a low molecular weight, nonphosphorus, nonpeptide, and highly selective inhibitor of protein-tyrosine phosphatase 1B. J. Biol. Chem. 275, 10300-10307 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 10300-10307
    • Iversen, L.F.1
  • 17
    • 0032562586 scopus 로고    scopus 로고
    • Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography
    • Pannifer, A.D., Flint, A.J., Tonks, N.K. & Barford, D. Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography. J. Biol. Chem. 273, 10454-10462 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10454-10462
    • Pannifer, A.D.1    Flint, A.J.2    Tonks, N.K.3    Barford, D.4
  • 18
    • 0029917244 scopus 로고    scopus 로고
    • Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis
    • Denu, J.M., Lohse, D.L., Vijayalakshmi, J., Saper, M.A. & Dixon, J.E. Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis. Proc. Natl. Acad. Sci. USA 93, 2493-2498 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2493-2498
    • Denu, J.M.1    Lohse, D.L.2    Vijayalakshmi, J.3    Saper, M.A.4    Dixon, J.E.5
  • 19
    • 0034604684 scopus 로고    scopus 로고
    • Down-regulation of insulin signaling by protein-tyrosine phosphatase 1B is mediated by an N-terminal binding region
    • Dadke, S., Kusari, J. & Chernoff, J. Down-regulation of insulin signaling by protein-tyrosine phosphatase 1B is mediated by an N-terminal binding region. J. Biol. Chem. 275, 23642-23647 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 23642-23647
    • Dadke, S.1    Kusari, J.2    Chernoff, J.3
  • 20
    • 0035873420 scopus 로고    scopus 로고
    • Small molecule peptidomimetics containing a novel phosphotyrosine bioisostere inhibit protein tyrosine phosphatase 1B and augment insulin action
    • Bleasdale, J.E. et al. Small molecule peptidomimetics containing a novel phosphotyrosine bioisostere inhibit protein tyrosine phosphatase 1B and augment insulin action. Biochemistry 40, 5642-5654 (2001).
    • (2001) Biochemistry , vol.40 , pp. 5642-5654
    • Bleasdale, J.E.1
  • 21
    • 10744223631 scopus 로고    scopus 로고
    • Cellular effects of small molecule PTP1B inhibitors on insulin signaling
    • Xie, L. et al. Cellular effects of small molecule PTP1B inhibitors on insulin signaling. Biochemistry 42, 12792-12804 (2003).
    • (2003) Biochemistry , vol.42 , pp. 12792-12804
    • Xie, L.1
  • 22
    • 0034507958 scopus 로고    scopus 로고
    • Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B
    • Salmeen, A., Andersen, J.N., Myers, M.P., Tonks, N.K. & Barford, D. Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B. Mol. Cell 6, 1401-1412 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1401-1412
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Tonks, N.K.4    Barford, D.5
  • 23
    • 0034710976 scopus 로고    scopus 로고
    • Can allosteric regulation be predicted from structure
    • Freire, E. Can allosteric regulation be predicted from structure. Proc. Natl. Acad. Sci. USA 97, 11680-11682 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11680-11682
    • Freire, E.1
  • 24
    • 0033642945 scopus 로고    scopus 로고
    • Structural stability of binding sites: Consequences for binding affinity and allosteric effects
    • Luque, I. & Freire, E. Structural stability of binding sites: consequences for binding affinity and allosteric effects. Proteins 41 (suppl.), 63-71 (2000).
    • (2000) Proteins , vol.41 , Issue.SUPPL. , pp. 63-71
    • Luque, I.1    Freire, E.2
  • 25
    • 0034785827 scopus 로고    scopus 로고
    • Structural and evolutionary relationships among protein tyrosine phosphatase domains
    • Andersen, J.N. et al. Structural and evolutionary relationships among protein tyrosine phosphatase domains. Mol. Cell. Biol. 21, 7117-7136 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7117-7136
    • Andersen, J.N.1
  • 26
    • 0030703139 scopus 로고    scopus 로고
    • The noncatalytic C-terminal segment of the T cell protein tyrosine phosphatase regulates activity via an intramolecular mechanism
    • Hao, L., Tiganis, T., Tonks, N.K. & Charbonneau, H. The noncatalytic C-terminal segment of the T cell protein tyrosine phosphatase regulates activity via an intramolecular mechanism. J. Biol. Chem. 272, 29322-29329 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 29322-29329
    • Hao, L.1    Tiganis, T.2    Tonks, N.K.3    Charbonneau, H.4
  • 27
    • 0025277449 scopus 로고
    • Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR
    • Streuli, M., Krueger, N.X., Thai, T., Tang, M. & Saito, H. Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. EMBO J. 9, 2399-2407 (1990).
    • (1990) EMBO J. , vol.9 , pp. 2399-2407
    • Streuli, M.1    Krueger, N.X.2    Thai, T.3    Tang, M.4    Saito, H.5
  • 28
    • 0033553515 scopus 로고    scopus 로고
    • Crystal structure of the tandem phosphatase domains of RPTP LAR
    • Nam, H.J., Poy, F., Krueger, N.X., Saito, H. & Frederick, C.A. Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell 97, 449-457 (1999).
    • (1999) Cell , vol.97 , pp. 449-457
    • Nam, H.J.1    Poy, F.2    Krueger, N.X.3    Saito, H.4    Frederick, C.A.5
  • 29
    • 0027223005 scopus 로고
    • Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: Identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation
    • Flint, A.J., Gebbink, M.F., Franza, B.R., Jr., Hill, D.E. & Tonks, N.K. Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation. EMBO J. 12, 1937-1946 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1937-1946
    • Flint, A.J.1    Gebbink, M.F.2    Franza Jr., B.R.3    Hill, D.E.4    Tonks, N.K.5
  • 30
    • 0029856493 scopus 로고    scopus 로고
    • Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)
    • Liu, F., Hill, D.E. & Chernoff, J. Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas). J. Biol. Chem. 271, 31290-31295 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 31290-31295
    • Liu, F.1    Hill, D.E.2    Chernoff, J.3
  • 31
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague, S.J. Implications of protein flexibility for drug discovery. Nat. Rev. Drug Discov. 2, 527-541 (2003).
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 527-541
    • Teague, S.J.1
  • 32
    • 0036490942 scopus 로고    scopus 로고
    • Allosteric binding sites on cell-surface receptors: Novel targets for drug discovery
    • Christopoulos, A. Allosteric binding sites on cell-surface receptors: Novel targets for drug discovery. Nat. Rev. Drug Discov. 1, 198-210 (2002).
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 198-210
    • Christopoulos, A.1
  • 33
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for ST1-571 inhibition of abelson tyrosine kinase
    • Schindler, T. et al. Structural mechanism for ST1-571 inhibition of abelson tyrosine kinase. Science 289, 1938-1942 (2000).
    • (2000) Science , vol.289 , pp. 1938-1942
    • Schindler, T.1
  • 34
    • 0036791512 scopus 로고    scopus 로고
    • Latest developments in crystallography and structure-based design of protein kinase inhibitors as drug candidates
    • Williams, D.H. & Mitchell, T. Latest developments in crystallography and structure-based design of protein kinase inhibitors as drug candidates. Curr. Opin. Pharmcol. 2, 1-7 (2002).
    • (2002) Curr. Opin. Pharmcol. , vol.2 , pp. 1-7
    • Williams, D.H.1    Mitchell, T.2
  • 35
    • 18344395134 scopus 로고    scopus 로고
    • Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
    • Pargellis, C. et al. Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nat. Struct. Biol. 9, 268-272 (2002).
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 268-272
    • Pargellis, C.1
  • 36
    • 0038274086 scopus 로고    scopus 로고
    • Discovery of a new phosphotyrosine mimetic for PTP1B using breakaway tethering
    • Erlanson, D.A. et al. Discovery of a new phosphotyrosine mimetic for PTP1B using breakaway tethering. J. Am. Chem. Soc. 125, 5602-5603 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5602-5603
    • Erlanson, D.A.1
  • 37
    • 0034629107 scopus 로고    scopus 로고
    • 2-(oxalylamino)-benzoic acid is a general, competitive inhibitor of protein-tyrosine phosphatases
    • Andersen, H.S. et al. 2-(oxalylamino)-benzoic acid is a general, competitive inhibitor of protein-tyrosine phosphatases. J. Biol. Chem. 275, 7101-7108 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 7101-7108
    • Andersen, H.S.1
  • 38
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J.W. The finer things in X-ray diffraction data collection. Acta Crystallogr. D 55, 1718-1725 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 40
    • 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. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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