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Science 23 June 1995:
Vol. 268. no. 5218, pp. 1754 - 1758
DOI: 10.1126/science.7540771
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Articles

Science, Vol 268, Issue 5218, 1754-1758
Copyright © 1995 by American Association for the Advancement of Science

articles

Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B

Z Jia, D Barford, AJ Flint, and NK Tonks

Laboratory of Molecular Biophysics, University of Oxford, UK.

The crystal structures of a cysteine-215-->serine mutant of protein tyrosine phosphatase 1B complexed with high-affinity peptide substrates corresponding to an autophosphorylation site of the epidermal growth factor receptor were determined. Peptide binding to the protein phosphatase was accompanied by a conformational change of a surface loop that created a phosphotyrosine recognition pocket and induced a catalytically competent form of the enzyme. The phosphotyrosine side chain is buried within the period and anchors the peptide substrate to its binding site. Hydrogen bonds between peptide main-chain atoms and the protein contribute to binding affinity, and specific interactions of acidic residues of the peptide with basic residues on the surface of the enzyme confer sequence specificity.


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Acquisition of a Specific and Potent PTP1B Inhibitor from a Novel Combinatorial Library and Screening Procedure.
K. Shen, Y.-F. Keng, L. Wu, X.-L. Guo, D. S. Lawrence, and Z.-Y. Zhang (2001)
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Site-selective Dephosphorylation of the Platelet-derived Growth Factor beta -Receptor by the Receptor-like Protein-tyrosine Phosphatase DEP-1.
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Structure-based Design of a Low Molecular Weight, Nonphosphorus, Nonpeptide, and Highly Selective Inhibitor of Protein-tyrosine Phosphatase 1B.
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C. C. Fjeld, A. E. Rice, Y. Kim, K. R. Gee, and J. M. Denu (2000)
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H. S. Andersen, L. F. Iversen, C. B. Jeppesen, S. Branner, K. Norris, H. B. Rasmussen, K. B. Moller, and N. P. H. Moller (2000)
J. Biol. Chem. 275, 7101-7108
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Structural Basis for Substrate Specificity of Protein-tyrosine Phosphatase SHP-1.
J. Yang, Z. Cheng, T. Niu, X. Liang, Z. J. Zhao, and G. W. Zhou (2000)
J. Biol. Chem. 275, 4066-4071
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Assessment of Protein-tyrosine Phosphatase 1B Substrate Specificity Using "Inverse Alanine Scanning".
S. W. Vetter, Y.-F. Keng, D. S. Lawrence, and Z.-Y. Zhang (2000)
J. Biol. Chem. 275, 2265-2268
   Abstract »    Full Text »    PDF »
Mechanism of Mitogen-activated Protein Kinase Phosphatase-3 Activation by ERK2.
B. Zhou and Z.-Y. Zhang (1999)
J. Biol. Chem. 274, 35526-35534
   Abstract »    Full Text »    PDF »
Role of PTP-1B in aortic smooth muscle cell motility and tyrosine phosphorylation of focal adhesion proteins.
A. Hassid, S. Huang, and J. Yao (1999)
Am J Physiol Heart Circ Physiol 277, H192-H198
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Direct High Affinity Modulation of Connexin Channel Activity by Cyclic Nucleotides.
C. G. Bevans and A. L. Harris (1999)
J. Biol. Chem. 274, 3720-3725
   Abstract »    Full Text »    PDF »
Interconversion of the Kinetic Identities of the Tandem Catalytic Domains of Receptor-like Protein-tyrosine Phosphatase PTPalpha by Two Point Mutations Is Synergistic and Substrate-dependent.
K. L. Lim, P. R. Kolatkar, K. P. Ng, C. H. Ng, and C. J. Pallen (1998)
J. Biol. Chem. 273, 28986-28993
   Abstract »    Full Text »    PDF »
SLP-76 Is a Direct Substrate of SHP-1 Recruited to Killer Cell Inhibitory Receptors.
B. A. Binstadt, D. D. Billadeau, B. L. Williams, N. Fang, T. Yi, G. A. Koretzky, R. T. Abraham, and P. J. Leibson (1998)
J. Biol. Chem. 273, 27518-27523
   Abstract »    Full Text »    PDF »
Molecular Basis for Substrate Specificity of Protein-tyrosine Phosphatase 1B.
M. Sarmiento, Y. Zhao, S. J. Gordon, and Z.-Y. Zhang (1998)
J. Biol. Chem. 273, 26368-26374
   Abstract »    Full Text »    PDF »
Crystal Structure of a Human Low Molecular Weight Phosphotyrosyl Phosphatase. IMPLICATIONS FOR SUBSTRATE SPECIFICITY.
M. Zhang, C. V. Stauffacher, D. Lin, and R. L. Van Etten (1998)
J. Biol. Chem. 273, 21714-21720
   Abstract »    Full Text »    PDF »
Identification of Major Binding Proteins and Substrates for the SH2-Containing Protein Tyrosine Phosphatase SHP-1 in Macrophages.
J. F. Timms, K. Carlberg, H. Gu, H. Chen, S. Kamatkar, M. J. S. Nadler, L. R. Rohrschneider, and B. G. Neel (1998)
Mol. Cell. Biol. 18, 3838-3850
   Abstract »    Full Text »
Suramin Is an Active Site-directed, Reversible, and Tight-binding Inhibitor of Protein-tyrosine Phosphatases.
Y.-L. Zhang, Y.-F. Keng, Y. Zhao, L. Wu, and Z.-Y. Zhang (1998)
J. Biol. Chem. 273, 12281-12287
   Abstract »    Full Text »    PDF »
Protein Tyrosine Phosphatase 1B Antagonizes Signalling by Oncoprotein Tyrosine Kinase p210 bcr-abl In Vivo.
K. R. LaMontagne Jr., A. J. Flint, B. R. Franza Jr., A. M. Pendergast, and N. K. Tonks (1998)
Mol. Cell. Biol. 18, 2965-2975
   Abstract »    Full Text »
Visualization of the Cysteinyl-phosphate Intermediate of a Protein-tyrosine Phosphatase by X-ray Crystallography.
A. D. B. Pannifer, A. J. Flint, N. K. Tonks, and D. Barford (1998)
J. Biol. Chem. 273, 10454-10462
   Abstract »    Full Text »    PDF »
The Mitogen-activated Protein Kinase Phosphatase-3 N-terminal Noncatalytic Region Is Responsible for Tight Substrate Binding and Enzymatic Specificity.
M. Muda, A. Theodosiou, C. Gillieron, A. Smith, C. Chabert, M. Camps, U. Boschert, N. Rodrigues, K. Davies, A. Ashworth, et al. (1998)
J. Biol. Chem. 273, 9323-9329
   Abstract »    Full Text »    PDF »
Altering the Nucleophile Specificity of a Protein-tyrosine Phosphatase-catalyzed Reaction. PROBING THE FUNCTION OF THE INVARIANT GLUTAMINE RESIDUES.
Y. Zhao, L. Wu, S. J. Noh, K.-L. Guan, and Z.-Y. Zhang (1998)
J. Biol. Chem. 273, 5484-5492
   Abstract »    Full Text »    PDF »
Identification of a Novel Polyproline Recognition Site in the Cytoskeletal Associated Protein, Proline Serine Threonine Phosphatase Interacting Protein.
D. Dowbenko, S. Spencer, C. Quan, and L. A. Lasky (1998)
J. Biol. Chem. 273, 989-996
   Abstract »    Full Text »    PDF »
Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design.
Y. A. Puius, Y. Zhao, M. Sullivan, D. S. Lawrence, S. C. Almo, and Z.-Y. Zhang (1997)
PNAS 94, 13420-13425
   Abstract »    Full Text »    PDF »
The Crystal Structure of Domain 1 of Receptor Protein-tyrosine Phosphatase µ.
K. M. V. Hoffmann, N. K. Tonks, and D. Barford (1997)
J. Biol. Chem. 272, 27505-27508
   Abstract »    Full Text »    PDF »
The Activity of Cdc14p, an Oligomeric Dual Specificity Protein Phosphatase from Saccharomyces cerevisiae, Is Required for Cell Cycle Progression.
G. S. Taylor, Y. Liu, C. Baskerville, and H. Charbonneau (1997)
J. Biol. Chem. 272, 24054-24063
   Abstract »    Full Text »    PDF »
PSTPIP: A Tyrosine Phosphorylated Cleavage Furrow-associated Protein that Is a Substrate for a PEST Tyrosine Phosphatase.
S. Spencer, D. Dowbenko, J. Cheng, W. Li, J. Brush, S. Utzig, V. Simanis, and L. A. Lasky (1997)
J. Cell Biol. 138, 845-860
   Abstract »    Full Text »    PDF »
Identification of in Vivo Phosphorylation Sites of CD45 Protein-tyrosine Phosphatase in 70Z/3.12 Cells.
S. Kang, P.-c. Liao, D. A. Gage, and W. J. Esselman (1997)
J. Biol. Chem. 272, 11588-11596
   Abstract »    Full Text »    PDF »
Protein-tyrosine Phosphatases PTP1B and Syp Are Modulators of Insulin-stimulated Translocation of GLUT4 in Transfected Rat Adipose Cells.
H. Chen, S. J. Wertheimer, C. H. Lin, S. L. Katz, K. E. Amrein, P. Burn, and M. J. Quon (1997)
J. Biol. Chem. 272, 8026-8031
   Abstract »    Full Text »    PDF »
A Novel Protein-Tyrosine Phosphatase Related to the Homotypically Adhering kappa andµReceptors.
J. Cheng, K. Wu, M. Armanini, N. O'Rourke, D. Dowbenko, and L. A. Lasky (1997)
J. Biol. Chem. 272, 7264-7277
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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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Protein-tyrosine Phosphatase 1B Is a Negative Regulator of Insulin- and Insulin-like Growth Factor-I-stimulated Signaling.
K. A. Kenner, E. Anyanwu, J. M. Olefsky, and J. Kusari (1996)
J. Biol. Chem. 271, 19810-19816
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The X-ray Crystal Structures of Yersinia Tyrosine Phosphatase with Bound Tungstate and Nitrate. MECHANISTIC IMPLICATIONS.
E. B. Fauman, C. Yuvaniyama, H. L. Schubert, J. A. Stuckey, and M. A. Saper (1996)
J. Biol. Chem. 271, 18780-18788
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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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
A Single Mutation Converts a Novel Phosphotyrosine Binding Domain into a Dual-specificity Phosphatase.
M. J. Wishart, J. M. Denu, J. A. Williams, and J. E. Dixon (1995)
J. Biol. Chem. 270, 26782-26785
   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 »
Calmodulin Binds to and Inhibits the Activity of the Membrane Distal Catalytic Domain of Receptor Protein-tyrosine Phosphatase alpha.
L. Liang, K. L. Lim, K. T. Seow, C. H. Ng, and C. J. Pallen (2000)
J. Biol. Chem. 275, 30075-30081
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Mechanism of Phosphoanhydride Cleavage by Baculovirus Phosphatase.
A. Martins and S. Shuman (2000)
J. Biol. Chem. 275, 35070-35076
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Inhibition of the Catalytic Activity of Cell Adhesion Kinase beta by Protein-tyrosine Phosphatase-PEST-mediated Dephosphorylation.
P. D. Lyons, J. M. Dunty, E. M. Schaefer, and M. D. Schaller (2001)
J. Biol. Chem. 276, 24422-24431
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The YRD Motif Is a Major Determinant of Substrate and Inhibitor Specificity in T-cell Protein-tyrosine Phosphatase.
E. Asante-Appiah, K. Ball, K. Bateman, K. Skorey, R. Friesen, C. Desponts, P. Payette, C. Bayly, R. Zamboni, G. Scapin, et al. (2001)
J. Biol. Chem. 276, 26036-26043
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The Mechanism of Dephosphorylation of Extracellular Signal-regulated Kinase 2 by Mitogen-activated Protein Kinase Phosphatase 3.
Y. Zhao and Z.-Y. Zhang (2001)
J. Biol. Chem. 276, 32382-32391
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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)
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