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Science 11 March 1994:
Vol. 263. no. 5152, pp. 1397 - 1404
DOI: 10.1126/science.8128219
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Articles

Science, Vol 263, Issue 5152, 1397-1404
Copyright © 1994 by American Association for the Advancement of Science

articles

Crystal structure of human protein tyrosine phosphatase 1B

D Barford, AJ Flint, and NK Tonks

W.M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, NY 11724.

Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues and are characterized by homologous catalytic domains. The crystal structure of a representative member of this family, the 37-kilodalton form (residues 1 to 321) of PTP1B, has been determined at 2.8 A resolution. The enzyme consists of a single domain with the catalytic site located at the base of a shallow cleft. The phosphate recognition site is created from a loop that is located at the amino-terminus of an alpha helix. This site is formed from an 11-residue sequence motif that is diagnostic of PTPs and the dual specificity phosphatases, and that contains the catalytically essential cysteine and arginine residues. The position of the invariant cysteine residue within the phosphate binding site is consistent with its role as a nucleophile in the catalytic reaction. The structure of PTP1B should serve as a model for other members of the PTP family and as a framework for understanding the mechanism of tyrosine dephosphorylation.


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M. Zhang, C. V. Stauffacher, D. Lin, and R. L. Van Etten (1998)
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S. W. Kang, I. C. Baines, and S. G. Rhee (1998)
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A Model for the Mechanism of Human Topoisomerase I.
L. Stewart, M. R. Redinbo, X. Qiu, W. G. Hol, and J. J. Champoux (1998)
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Active Site Titration of the Tyrosine Phosphatases SHP-1 and PTP1B Using Aromatic Disulfides. REACTION WITH THE ESSENTIAL CYSTEINE RESIDUE IN THE ACTIVE SITE.
M. J. Pregel and A. C. Storer (1997)
J. Biol. Chem. 272, 23552-23558
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P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase.
M. P. Myers, J. P. Stolarov, C. Eng, J. Li, S. I. Wang, M. H. Wigler, R. Parsons, and N. K. Tonks (1997)
PNAS 94, 9052-9057
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Antilipolytic Actions of Vanadate and Insulin in Rat Adipocytes Mediated by Distinctly Different Mechanisms.
J. Li, G. Elberg, N. Sekar, Z. B. He, and Y. Shechter (1997)
Endocrinology 138, 2274-2279
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Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases.
A. J. Flint, T. Tiganis, D. Barford, and N. K. Tonks (1997)
PNAS 94, 1680-1685
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Protein-Tyrosine Phosphatase 1B Complexes with the Insulin Receptor in Vivo and Is Tyrosine-phosphorylated in the Presence of Insulin.
D. Bandyopadhyay, A. Kusari, K. A. Kenner, F. Liu, J. Chernoff, T. A. Gustafson, and J. Kusari (1997)
J. Biol. Chem. 272, 1639-1645
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Purification and Kinetic Characterization of the Mitogen-activated Protein Kinase Phosphatase rVH6.
A. M. Wiland, J. M. Denu, R. J. Mourey, and J. E. Dixon (1996)
J. Biol. Chem. 271, 33486-33492
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Molecular Cloning of Phogrin, a Protein-tyrosine Phosphatase Homologue Localized to Insulin Secretory Granule Membranes.
C. Wasmeier and J. C. Hutton (1996)
J. Biol. Chem. 271, 18161-18170
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Determinants of Substrate Recognition in the Protein-tyrosine Phosphatase, PTP1.
Z.-Y. Zhang, A. B. Walsh, L. Wu, D. J. McNamara, E. M. Dobrusin, and W. T. Miller (1996)
J. Biol. Chem. 271, 5386-5392
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Roles of Active Site Residues and the NH(2)-terminal Domain in the Catalysis and Substrate Binding of Human Cdc25.
X. Xu and S. P. Burke (1996)
J. Biol. Chem. 271, 5118-5124
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The Active Site Specificity of the Yersinia Protein-tyrosine Phosphatase.
D. Dunn, L. Chen, D. S. Lawrence, and Z.-Y. Zhang (1996)
J. Biol. Chem. 271, 168-173
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The Yeast Immunophilin Fpr3 Is a Physiological Substrate of the Tyrosine-specific Phosphoprotein Phosphatase Ptp1.
L. K. Wilson, B. M. Benton, S. Zhou, J. Thorner, and G. S. Martin (1995)
J. Biol. Chem. 270, 25185-25193
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Identification of a Putative Syp Substrate, the PDGFbeta Receptor.
R. A. Klinghoffer and A. Kazlauskas (1995)
J. Biol. Chem. 270, 22208-22217
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Cloning and Characterization of a Saccharomyces cerevisiae Gene Encoding the Low Molecular Weight Protein-tyrosine Phosphatase.
K. Ostanin, C. Pokalsky, S. Wang, and R. L. Van Etten (1995)
J. Biol. Chem. 270, 18491-18499
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Are Protein-tyrosine Phosphatases Specific for Phosphotyrosine?.
Z.-Y. Zhang and Z. Y. Zhang (1995)
J. Biol. Chem. 270, 16052-16055
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Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases.
P Dent, T Jelinek, D. Morrison, M. Weber, and T. Sturgill (1995)
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Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B.
Z Jia, D Barford, A. Flint, and N. Tonks (1995)
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The Blockade of Preadipocyte Differentiation by Protein-tyrosine Phosphatase HA2 Is Reversed by Vanadate.
K. Liao and M. D. Lane (1995)
J. Biol. Chem. 270, 12123-12132
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The Extraordinary Active Site Substrate Specificity of pp60[IMAGE][IMAGE].
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J. Biol. Chem. 270, 5375-5380
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Multiple Dual Specificity Protein Tyrosine Phosphatases Are Expressed and Regulated Differentially in Liver Cell Lines.
S. P. Kwak and J. E. Dixon (1995)
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   Abstract »    Full Text »    PDF »
Predicting protein crystal structures.
S. Benner, D. Gerloff, and T. Jenny (1994)
Science 265, 1642-1644
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Taking a first look at a tyrosine phosphatase.
J Marx (1994)
Science 263, 1373
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Down-regulation of Insulin Signaling by Protein-tyrosine Phosphatase 1B Is Mediated by an N-terminal Binding Region.
S. Dadke, J. Kusari, and J. Chernoff (2000)
J. Biol. Chem. 275, 23642-23647
   Abstract »    Full Text »    PDF »
Identification of p130cas as an in Vivo Substrate of Receptor Protein-tyrosine Phosphatase alpha.
A. Buist, C. Blanchetot, L. G. J. Tertoolen, and J. den Hertog (2000)
J. Biol. Chem. 275, 20754-20761
   Abstract »    Full Text »    PDF »
Thermodynamic Study of Ligand Binding to Protein-tyrosine Phosphatase 1B and Its Substrate-trapping Mutants.
Y.-L. Zhang, Z.-J. Yao, M. Sarmiento, L. Wu, T. R. Burke Jr., and Z.-Y. Zhang (2000)
J. Biol. Chem. 275, 34205-34212
   Abstract »    Full Text »    PDF »
1-Cys Peroxiredoxin, a Bifunctional Enzyme with Glutathione Peroxidase and Phospholipase A2 Activities.
J.-W. Chen, C. Dodia, S. I. Feinstein, M. K. Jain, and A. B. Fisher (2000)
J. Biol. Chem. 275, 28421-28427
   Abstract »    Full Text »    PDF »
Inhibitory Role for Dual Specificity Phosphatase VHR in T Cell Antigen Receptor and CD28-induced Erk and Jnk Activation.
A. Alonso, M. Saxena, S. Williams, and T. Mustelin (2001)
J. Biol. Chem. 276, 4766-4771
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Mutational and Kinetic Evaluation of Conserved His-123 in Dual Specificity Protein-tyrosine Phosphatase Vaccinia H1-related Phosphatase. PARTICIPATION OF TYR-78 AND THR-73 RESIDUES IN TUNING THE ORIENTATION OF HIS-123.
J.-H. Kim, D. Y. Shin, M.-H. Han, and M.-U. Choi (2001)
J. Biol. Chem. 276, 27568-27574
   Abstract »    Full Text »    PDF »
Characterization of the Net1 Cell Cycle-dependent Regulator of the Cdc14 Phosphatase from Budding Yeast.
E. E. Traverso, C. Baskerville, Y. Liu, W. Shou, P. James, R. J. Deshaies, and H. Charbonneau (2001)
J. Biol. Chem. 276, 21924-21931
   Abstract »    Full Text »    PDF »
The Phosphatase C(X)5R Motif Is Required for Catalytic Activity of the Saccharomyces cerevisiae Acr2p Arsenate Reductase.
R. Mukhopadhyay and B. P. Rosen (2001)
J. Biol. Chem. 276, 34738-34742
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Insulin Stimulates Tyrosine Phosphorylation and Inactivation of Protein-tyrosine Phosphatase 1B in Vivo.
J. Tao, C. C. Malbon, and H.-y. Wang (2001)
J. Biol. Chem. 276, 29520-29525
   Abstract »    Full Text »    PDF »
Residue 259 Is a Key Determinant of Substrate Specificity of Protein-tyrosine Phosphatases 1B and alpha.
G. H. Peters, L. F. Iversen, S. Branner, H. S. Andersen, S. B. Mortensen, O. H. Olsen, K. B. Moller, and N. P. H. Moller (2000)
J. Biol. Chem. 275, 18201-18209
   Abstract »    Full Text »    PDF »
Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases.
M. S. Bennett, Z. Guan, M. Laurberg, and X.-D. Su (2001)
PNAS 98, 13577-13582
   Abstract »    Full Text »    PDF »


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