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Crystal structure of the tyrosine phosphatase SHP-2.

Hof P, Pluskey S, Dhe-Paganon S, Eck MJ, Shoelson SE
Cell 92 441-50 (1998)
Cited: 537 times
EuropePMC logo PMID: 9491886

Abstract

The structure of the SHP-2 tyrosine phosphatase, determined at 2.0 angstroms resolution, shows how its catalytic activity is regulated by its two SH2 domains. In the absence of a tyrosine-phosphorylated binding partner, the N-terminal SH2 domain binds the phosphatase domain and directly blocks its active site. This interaction alters the structure of the N-SH2 domain, disrupting its phosphopeptide-binding cleft. Conversely, interaction of the N-SH2 domain with phosphopeptide disrupts its phosphatase recognition surface. Thus, the N-SH2 domain is a conformational switch; it either binds and inhibits the phosphatase, or it binds phosphoproteins and activates the enzyme. Recognition of bisphosphorylated ligands by the tandem SH2 domains is an integral element of this switch; the C-terminal SH2 domain contributes binding energy and specificity, but it does not have a direct role in activation.

Reviews - 2shp mentioned but not cited (10)

  1. Targeting protein tyrosine phosphatases for anticancer drug discovery. Scott LM, Lawrence HR, Sebti SM, Lawrence NJ, Wu J. Curr Pharm Des 16 1843-1862 (2010)
  2. Perspectives for the use of structural information and chemical genetics to develop inhibitors of Janus kinases. Haan C, Behrmann I, Haan S. J Cell Mol Med 14 504-527 (2010)
  3. Tyrosine phosphatase SHP2 inhibitors in tumor-targeted therapies. Song Z, Wang M, Ge Y, Chen XP, Xu Z, Sun Y, Xiong XF. Acta Pharm Sin B 11 13-29 (2021)
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  6. Immune Checkpoint Receptors Signaling in T Cells. Baldanzi G. Int J Mol Sci 23 3529 (2022)
  7. Regulation of Brain-Derived Neurotrophic Factor and Growth Factor Signaling Pathways by Tyrosine Phosphatase Shp2 in the Retina: A Brief Review. Abbasi M, Gupta V, Chitranshi N, You Y, Dheer Y, Mirzaei M, Graham SL. Front Cell Neurosci 12 85 (2018)
  8. Recent advances in the discovery of protein tyrosine phosphatase SHP2 inhibitors. Kong J, Long YQ. RSC Med Chem 13 246-257 (2022)
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Articles - 2shp mentioned but not cited (54)

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  5. Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains. Sha F, Gencer EB, Georgeon S, Koide A, Yasui N, Koide S, Hantschel O. Proc Natl Acad Sci U S A 110 14924-14929 (2013)
  6. Structural and mechanistic insights into LEOPARD syndrome-associated SHP2 mutations. Yu ZH, Xu J, Walls CD, Chen L, Zhang S, Zhang R, Wu L, Wang L, Liu S, Zhang ZY. J Biol Chem 288 10472-10482 (2013)
  7. Structural reorganization of SHP2 by oncogenic mutations and implications for oncoprotein resistance to allosteric inhibition. LaRochelle JR, Fodor M, Vemulapalli V, Mohseni M, Wang P, Stams T, LaMarche MJ, Chopra R, Acker MG, Blacklow SC. Nat Commun 9 4508 (2018)
  8. A tandem SH2 domain in transcription elongation factor Spt6 binds the phosphorylated RNA polymerase II C-terminal repeat domain (CTD). Sun M, Larivière L, Dengl S, Mayer A, Cramer P. J Biol Chem 285 41597-41603 (2010)
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  12. Inhibitors of Src homology-2 domain containing protein tyrosine phosphatase-2 (Shp2) based on oxindole scaffolds. Lawrence HR, Pireddu R, Chen L, Luo Y, Sung SS, Szymanski AM, Yip ML, Guida WC, Sebti SM, Wu J, Lawrence NJ. J Med Chem 51 4948-4956 (2008)
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  15. Structural insights into Noonan/LEOPARD syndrome-related mutants of protein-tyrosine phosphatase SHP2 (PTPN11). Qiu W, Wang X, Romanov V, Hutchinson A, Lin A, Ruzanov M, Battaile KP, Pai EF, Neel BG, Chirgadze NY. BMC Struct Biol 14 10 (2014)
  16. Identification of cryptotanshinone as an inhibitor of oncogenic protein tyrosine phosphatase SHP2 (PTPN11). Liu W, Yu B, Xu G, Xu WR, Loh ML, Tang LD, Qu CK. J Med Chem 56 7212-7221 (2013)
  17. Structural and Functional Consequences of Three Cancer-Associated Mutations of the Oncogenic Phosphatase SHP2. LaRochelle JR, Fodor M, Xu X, Durzynska I, Fan L, Stams T, Chan HM, LaMarche MJ, Chopra R, Wang P, Fortin PD, Acker MG, Blacklow SC. Biochemistry 55 2269-2277 (2016)
  18. Identification of small molecular weight inhibitors of Src homology 2 domain-containing tyrosine phosphatase 2 (SHP-2) via in silico database screening combined with experimental assay. Yu WM, Guvench O, Mackerell AD, Qu CK. J Med Chem 51 7396-7404 (2008)
  19. Structural mechanism associated with domain opening in gain-of-function mutations in SHP2 phosphatase. Darian E, Guvench O, Yu B, Qu CK, MacKerell AD. Proteins 79 1573-1588 (2011)
  20. Counteracting effects operating on Src homology 2 domain-containing protein-tyrosine phosphatase 2 (SHP2) function drive selection of the recurrent Y62D and Y63C substitutions in Noonan syndrome. Martinelli S, Nardozza AP, Delle Vigne S, Sabetta G, Torreri P, Bocchinfuso G, Flex E, Venanzi S, Palleschi A, Gelb BD, Cesareni G, Stella L, Castagnoli L, Tartaglia M. J Biol Chem 287 27066-27077 (2012)
  21. Critical role of Shp2 in tumor growth involving regulation of c-Myc. Ren Y, Chen Z, Chen L, Fang B, Win-Piazza H, Haura E, Koomen JM, Wu J. Genes Cancer 1 994-1007 (2010)
  22. Inhibition of cellular Shp2 activity by a methyl ester analog of SPI-112. Chen L, Pernazza D, Scott LM, Lawrence HR, Ren Y, Luo Y, Wu X, Sung SS, Guida WC, Sebti SM, Lawrence NJ, Wu J. Biochem Pharmacol 80 801-810 (2010)
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  24. Phosphotyrosine couples peptide binding and SHP2 activation via a dynamic allosteric network. Marasco M, Kirkpatrick J, Nanna V, Sikorska J, Carlomagno T. Comput Struct Biotechnol J 19 2398-2415 (2021)
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  26. Receptor tyrosine kinase ubiquitylation involves the dynamic regulation of Cbl-Spry2 by intersectin 1 and the Shp2 tyrosine phosphatase. Okur MN, Russo A, O'Bryan JP. Mol Cell Biol 34 271-279 (2014)
  27. Targeting Oncogenic Src Homology 2 Domain-Containing Phosphatase 2 (SHP2) by Inhibiting Its Protein-Protein Interactions. Bobone S, Pannone L, Biondi B, Solman M, Flex E, Canale VC, Calligari P, De Faveri C, Gandini T, Quercioli A, Torini G, Venditti M, Lauri A, Fasano G, Hoeksma J, Santucci V, Cattani G, Bocedi A, Carpentieri G, Tirelli V, Sanchez M, Peggion C, Formaggio F, den Hertog J, Martinelli S, Bocchinfuso G, Tartaglia M, Stella L. J Med Chem 64 15973-15990 (2021)
  28. Structural Determinants of Phosphopeptide Binding to the N-Terminal Src Homology 2 Domain of the SHP2 Phosphatase. Anselmi M, Calligari P, Hub JS, Tartaglia M, Bocchinfuso G, Stella L. J Chem Inf Model 60 3157-3171 (2020)
  29. A specific amino acid context in EGFR and HER2 phosphorylation sites enables selective binding to the active site of Src homology phosphatase 2 (SHP2). Hartman Z, Geldenhuys WJ, Agazie YM. J Biol Chem 295 3563-3575 (2020)
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  34. brief-report SHP2 Inhibition Sensitizes Diverse Oncogene-Addicted Solid Tumors to Re-treatment with Targeted Therapy. Drilon A, Sharma MR, Johnson ML, Yap TA, Gadgeel S, Nepert D, Feng G, Reddy MB, Harney AS, Elsayed M, Cook AW, Wong CE, Hinklin RJ, Jiang Y, Brown EN, Neitzel NA, Laird ER, Wu WI, Singh A, Wei P, Ching KA, Gaudino JJ, Lee PA, Hartley DP, Rothenberg SM. Cancer Discov 13 1789-1801 (2023)
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  36. A multifunctional cross-validation high-throughput screening protocol enabling the discovery of new SHP2 inhibitors. Song Y, Zhao M, Wu Y, Yu B, Liu HM. Acta Pharm Sin B 11 750-762 (2021)
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  38. Noonan Syndrome in South Africa: Clinical and Molecular Profiles. Tekendo-Ngongang C, Agenbag G, Bope CD, Esterhuizen AI, Wonkam A. Front Genet 10 333 (2019)
  39. Protein Kinase A (PKA) Phosphorylation of Shp2 Protein Inhibits Its Phosphatase Activity and Modulates Ligand Specificity. Burmeister BT, Wang L, Gold MG, Skidgel RA, O'Bryan JP, Carnegie GK. J Biol Chem 290 12058-12067 (2015)
  40. SHP2 allosteric inhibitor TK-453 alleviates psoriasis-like skin inflammation in mice via inhibition of IL-23/Th17 axis. Wang M, Li T, Ouyang Z, Tang K, Zhu Y, Song C, Sun H, Yu B, Ji X, Sun Y. iScience 25 104009 (2022)
  41. Determining folding and binding properties of the C-terminal SH2 domain of SHP2. Nardella C, Malagrinò F, Pagano L, Rinaldo S, Gianni S, Toto A. Protein Sci 30 2385-2395 (2021)
  42. Discriminating between competing models for the allosteric regulation of oncogenic phosphatase SHP2 by characterizing its active state. Calligari P, Santucci V, Stella L, Bocchinfuso G. Comput Struct Biotechnol J 19 6125-6139 (2021)
  43. The loops of the N-SH2 binding cleft do not serve as allosteric switch in SHP2 activation. Anselmi M, Hub JS. Proc Natl Acad Sci U S A 118 e2025107118 (2021)
  44. The Influence of Molecular Reach and Diffusivity on the Efficacy of Membrane-Confined Reactions. Zhang Y, Clemens L, Goyette J, Allard J, Dushek O, Isaacson SA. Biophys J 117 1189-1201 (2019)
  45. Direct Chemical Activation of a Rationally Engineered Signaling Enzyme. Chio CM, Cheng KW, Bishop AC. Chembiochem 16 1735-1739 (2015)
  46. Discovery of the SHP2 allosteric inhibitor 2-((3R,4R)-4-amino-3-methyl-2-oxa-8-azaspiro[4.5]decan-8-yl)-5-(2,3-dichlorophenyl)-3-methylpyrrolo[2,1-f][1,2,4] triazin-4(3H)-one. Luo Y, Li J, Zong Y, Sun M, Zheng W, Zhu J, Liu L, Liu B. J Enzyme Inhib Med Chem 38 398-404 (2023)
  47. SHP2 regulates adipose maintenance and adipocyte-pancreatic cancer cell crosstalk via PDHA1. Olou AA, Ambrose J, Jack JL, Walsh M, Ruckert MT, Eades AE, Bye BA, Dandawate P, VanSaun MN. J Cell Commun Signal 17 575-590 (2023)
  48. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)
  49. The structural insights of stem cell factor receptor (c-Kit) interaction with tyrosine phosphatase-2 (Shp-2): an in silico analysis. Pati S, Gurudutta GU, Kalra OP, Mukhopadhyay A. BMC Res Notes 3 14 (2010)
  50. CARDIO-PRED: an in silico tool for predicting cardiovascular-disorder associated proteins. Jain P, Thukral N, Gahlot LK, Hasija Y. Syst Synth Biol 9 55-66 (2015)
  51. How a single mutation alters the protein structure: a simulation investigation on protein tyrosine phosphatase SHP2. Hou Y, Lu X, Xu Z, Qu J, Huang J. RSC Adv 13 4263-4274 (2023)
  52. Intramolecular Interaction with the E6 Region Stabilizes the Closed Conformation of the N-SH2 Domain and Concurs with the Self-Inhibitory Docking in Downregulating the Activity of the SHP2 Tyrosine Phosphatase: A Molecular Dynamics Study. Bellacchio E. Int J Mol Sci 23 4794 (2022)
  53. Monobody Inhibitor Selective to the Phosphatase Domain of SHP2 and its Use as a Probe for Quantifying SHP2 Allosteric Regulation. Sha F, Kurosawa K, Glasser E, Ketavarapu G, Albazzaz S, Koide A, Koide S. J Mol Biol 435 168010 (2023)
  54. Structure of cytotoxic associated antigen A protein of Helicobacter pylori from Bali and Lombok isolates of Indonesia. Suharsono H, Wibawa DN, Muttaqin Z, Agustina KK. Vet World 13 1319-1326 (2020)


Reviews citing this publication (135)

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