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Volumn 79, Issue 5, 2011, Pages 1573-1588

Structural mechanism associated with domain opening in gain-of-function mutations in SHP2 phosphatase

Author keywords

CHARMM; Childhood leukemia; Molecular dynamics; Noonan's syndrome; Normal mode analysis; Phosphatase assay; Potential of mean force

Indexed keywords

ARGININE; PHOSPHOPEPTIDE; PROTEIN TYROSINE PHOSPHATASE SHP 2;

EID: 79954624505     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22984     Document Type: Article
Times cited : (32)

References (52)
  • 1
    • 0030049783 scopus 로고    scopus 로고
    • Multiple requirements for SHPTP2 in epidermal growth factor-mediated cell cycle progression
    • Bennett AM, Hausdorff SF, O'Reilly AM, Freeman RM, Neel BG. Multiple requirements for SHPTP2 in epidermal growth factor-mediated cell cycle progression. Mol Cell Biol 1996; 16: 1189-1202.
    • (1996) Mol Cell Biol , vol.16 , pp. 1189-1202
    • Bennett, A.M.1    Hausdorff, S.F.2    O'Reilly, A.M.3    Freeman, R.M.4    Neel, B.G.5
  • 3
    • 0028933979 scopus 로고
    • The phosphotyrosine phosphatase PTP1D, but not PTP1C, is an essential mediator of fibroblast proliferation induced by tyrosine kinase and G protein-coupled receptors
    • Rivard N, McKenzie FR, Brondello JM, Pouyssegur J. The phosphotyrosine phosphatase PTP1D, but not PTP1C, is an essential mediator of fibroblast proliferation induced by tyrosine kinase and G protein-coupled receptors. J Biol Chem 1995; 270: 11017-11024.
    • (1995) J Biol Chem , vol.270 , pp. 11017-11024
    • Rivard, N.1    McKenzie, F.R.2    Brondello, J.M.3    Pouyssegur, J.4
  • 4
    • 33749376770 scopus 로고    scopus 로고
    • The scaffolding adapter Gab2, via Shp-2, regulates kit-evoked mast cell proliferation by activating the Rac/JNK pathway
    • Yu M, Luo J, Yang W, Wang Y, Mizuki M, Kanakura Y, Besmer P, Neel BG, Gu H. The scaffolding adapter Gab2, via Shp-2, regulates kit-evoked mast cell proliferation by activating the Rac/JNK pathway. J Biol Chem 2006; 281: 28615-28626.
    • (2006) J Biol Chem , vol.281 , pp. 28615-28626
    • Yu, M.1    Luo, J.2    Yang, W.3    Wang, Y.4    Mizuki, M.5    Kanakura, Y.6    Besmer, P.7    Neel, B.G.8    Gu, H.9
  • 5
    • 0038771965 scopus 로고    scopus 로고
    • The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
    • Neel BG, Gu H, Pao L. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem Sci 2003; 28: 284-293.
    • (2003) Trends Biochem Sci , vol.28 , pp. 284-293
    • Neel, B.G.1    Gu, H.2    Pao, L.3
  • 6
    • 42649118836 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the JAK/STAT pathway
    • Xu D, Qu CK. Protein tyrosine phosphatases in the JAK/STAT pathway. Front Biosci 2008; 13: 4925-4932.
    • (2008) Front Biosci , vol.13 , pp. 4925-4932
    • Xu, D.1    Qu, C.K.2
  • 7
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: from genes, to function, to disease
    • Tonks NK. Protein tyrosine phosphatases: from genes, to function, to disease. Nat Rev Mol Cell Biol 2006; 7: 833-846.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 9
    • 47249118481 scopus 로고    scopus 로고
    • Noonan syndrome-associated SHP-2/Ptpn11 mutants enhance SIRPalpha and PZR tyrosyl phosphorylation and promote adhesion-mediated ERK activation
    • Eminaga S, Bennett AM. Noonan syndrome-associated SHP-2/Ptpn11 mutants enhance SIRPalpha and PZR tyrosyl phosphorylation and promote adhesion-mediated ERK activation. J Biol Chem 2008; 283: 15328-15338.
    • (2008) J Biol Chem , vol.283 , pp. 15328-15338
    • Eminaga, S.1    Bennett, A.M.2
  • 13
    • 0027432407 scopus 로고
    • Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor
    • Lechleider RJ, Sugimoto S, Bennett AM, Kashishian AS, Cooper JA, Shoelson SE, Walsh CT, Neel BG. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. J Biol Chem 1993; 268: 21478-21481.
    • (1993) J Biol Chem , vol.268 , pp. 21478-21481
    • Lechleider, R.J.1    Sugimoto, S.2    Bennett, A.M.3    Kashishian, A.S.4    Cooper, J.A.5    Shoelson, S.E.6    Walsh, C.T.7    Neel, B.G.8
  • 14
    • 0028282967 scopus 로고
    • Activation of the SH2-containing protein tyrosine phosphatase. SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1
    • Sugimoto S, Wandless TJ, Shoelson SE, Neel BG, Walsh CT. Activation of the SH2-containing protein tyrosine phosphatase. SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1 J Biol Chem 1994; 269: 13614-13622.
    • (1994) J Biol Chem , vol.269 , pp. 13614-13622
    • Sugimoto, S.1    Wandless, T.J.2    Shoelson, S.E.3    Neel, B.G.4    Walsh, C.T.5
  • 16
    • 0030066325 scopus 로고    scopus 로고
    • Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2
    • Eck MJ, Pluskey S, Trub T, Harrison SC, Shoelson SE. Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2. Nature 1996; 379: 277-280.
    • (1996) Nature , vol.379 , pp. 277-280
    • Eck, M.J.1    Pluskey, S.2    Trub, T.3    Harrison, S.C.4    Shoelson, S.E.5
  • 17
    • 0032521428 scopus 로고    scopus 로고
    • Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2
    • Barford D, Neel BG. Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2. Structure 1998; 6: 249-254.
    • (1998) Structure , vol.6 , pp. 249-254
    • Barford, D.1    Neel, B.G.2
  • 18
    • 34047192313 scopus 로고    scopus 로고
    • Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft
    • Guvench O, Qu C-K, MacKerell ADJr. Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft. BMC Struct Biol 2007; 7: 14.
    • (2007) BMC Struct Biol , vol.7 , pp. 14
    • Guvench, O.1    Qu, C.-K.2    MacKerell Jr, A.D.3
  • 22
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • MacKerell ADJr, Feig M, Brooks CLIII. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comput Chem 2004; 25: 1400-1415.
    • (2004) J Comput Chem , vol.25 , pp. 1400-1415
    • MacKerell Jr, A.D.1    Feig, M.2    Brooks III, C.L.3
  • 23
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Do RKG, Sali A. Modeling of loops in protein structures. Protein Sci 2000; 9: 1753-1773.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.G.2    Sali, A.3
  • 24
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 1993; 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 26
    • 0014675222 scopus 로고
    • Refinement of protein conformations using a macromolecular energy minimization procedure
    • Levitt M, Lifson S. Refinement of protein conformations using a macromolecular energy minimization procedure. J Mol Biol 1969; 46: 269-279.
    • (1969) J Mol Biol , vol.46 , pp. 269-279
    • Levitt, M.1    Lifson, S.2
  • 27
    • 0000615669 scopus 로고
    • Function minimization by conjugate gradients
    • Fletcher R, Reeves C. Function minimization by conjugate gradients. Comput J 1964; 7: 149-154.
    • (1964) Comput J , vol.7 , pp. 149-154
    • Fletcher, R.1    Reeves, C.2
  • 28
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word JM, Lovell SC, Richardson JS, Richardson DC. Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J Mol Biol 1999; 285: 1735-1747.
    • (1999) J Mol Biol , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 30
    • 33751157933 scopus 로고
    • Solvent-induced forces between two hydrophilic groups
    • Durell SR, Brooks BR, Ben-Naim A. Solvent-induced forces between two hydrophilic groups. J Phys Chem 1994; 98: 2198-2202.
    • (1994) J Phys Chem , vol.98 , pp. 2198-2202
    • Durell, S.R.1    Brooks, B.R.2    Ben-Naim, A.3
  • 32
    • 33846823909 scopus 로고
    • Particle mesh Ewald: an N log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle mesh Ewald: an N log(N) method for Ewald sums in large systems. J Chem Phys 1993; 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 33
    • 84986534166 scopus 로고
    • New spherical-cutoff methods for long-range forces in macromolecular simulation
    • Steinbach PJ, Brooks BR. New spherical-cutoff methods for long-range forces in macromolecular simulation. J Comput Chem 1994; 15: 667-683.
    • (1994) J Comput Chem , vol.15 , pp. 667-683
    • Steinbach, P.J.1    Brooks, B.R.2
  • 34
    • 33646940952 scopus 로고
    • Numerical integration of Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC. Numerical integration of Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 1977; 23: 327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 35
    • 0000432120 scopus 로고
    • The potential calculation and some applications
    • In: Alder B,Fernbach S,Rotenberg M, editors. Methods in computational physics, New York: Academic Press.
    • Hockney RW. The potential calculation and some applications. In: Alder B, Fernbach S, Rotenberg M, editors. Methods in computational physics, Vol. 9. New York: Academic Press; 1970. pp 136-211.
    • (1970) , vol.9 , pp. 136-211
    • Hockney, R.W.1
  • 36
    • 0001538909 scopus 로고
    • Canonical dynamics: equilibrium phase-space distributions
    • Hoover WG. Canonical dynamics: equilibrium phase-space distributions. Phys Rev A 1985; 31: 1695-1697.
    • (1985) Phys Rev A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 37
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • Nosé S. A molecular dynamics method for simulations in the canonical ensemble. Mol Phys 1984; 52: 255-268.
    • (1984) Mol Phys , vol.52 , pp. 255-268
    • Nosé, S.1
  • 38
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: the Langevin piston method
    • Feller SE, Zhang YH, Pastor RW, Brooks BR. Constant pressure molecular dynamics simulation: the Langevin piston method. J Chem Phys 1995; 103: 4613-4621.
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.H.2    Pastor, R.W.3    Brooks, B.R.4
  • 39
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • Kumar S, Bouzida D, Swendsen RH, Kollman PA, Rosenberg JM. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J Comput Chem 1992; 13: 1011-1021.
    • (1992) J Comput Chem , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 40
    • 84860221627 scopus 로고    scopus 로고
    • Grossfield A. "WHAM: the weighted histogram analysis method", Version 2.0.3
    • Grossfield A. "WHAM: the weighted histogram analysis method", Version 2.0.3
  • 42
    • 0028322113 scopus 로고
    • Purification and characterization of PTP2C, a widely distributed protein tyrosine phosphatase containing two SH2 domains
    • Zhao Z, Larocque R, Ho WT, Fischer EH, Shen SH. Purification and characterization of PTP2C, a widely distributed protein tyrosine phosphatase containing two SH2 domains. J Biol Chem 1994; 269: 8780-8785.
    • (1994) J Biol Chem , vol.269 , pp. 8780-8785
    • Zhao, Z.1    Larocque, R.2    Ho, W.T.3    Fischer, E.H.4    Shen, S.H.5
  • 43
    • 0030797548 scopus 로고    scopus 로고
    • A deletion mutation in the SH2-N domain of Shp-2 severely suppresses hematopoietic cell development
    • Qu CK, Shi ZQ, Shen R, Tsai FY, Orkin SH, Feng GS. A deletion mutation in the SH2-N domain of Shp-2 severely suppresses hematopoietic cell development. Mol Cell Biol 1997; 17: 5499-5507.
    • (1997) Mol Cell Biol , vol.17 , pp. 5499-5507
    • Qu, C.K.1    Shi, Z.Q.2    Shen, R.3    Tsai, F.Y.4    Orkin, S.H.5    Feng, G.S.6
  • 44
    • 27644462900 scopus 로고    scopus 로고
    • The N-terminal end of the catalytic domain of SRC kinase Hck is a conformational switch implicated in long-range allosteric regulation
    • Banavali NK, Roux B. The N-terminal end of the catalytic domain of SRC kinase Hck is a conformational switch implicated in long-range allosteric regulation. Structure 2005; 13: 1715-1723.
    • (2005) Structure , vol.13 , pp. 1715-1723
    • Banavali, N.K.1    Roux, B.2
  • 45
    • 0037422594 scopus 로고    scopus 로고
    • Protein-facilitated base flipping in DNA by cytosine-5-methyltransferase
    • Huang N, Banavali NK, MacKerell ADJr. Protein-facilitated base flipping in DNA by cytosine-5-methyltransferase. Proc Natl Acad Sci USA 2003; 100: 68-73.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 68-73
    • Huang, N.1    Banavali, N.K.2    MacKerell Jr, A.D.3
  • 46
    • 31444443924 scopus 로고    scopus 로고
    • NMR imino proton exchange experiments on duplex DNA primarily monitor the opening of purine bases
    • Priyakumar UD, Mackerell ADJr. NMR imino proton exchange experiments on duplex DNA primarily monitor the opening of purine bases. J Am Chem Soc 2006; 128: 678-679.
    • (2006) J Am Chem Soc , vol.128 , pp. 678-679
    • Priyakumar, U.D.1    Mackerell Jr, A.D.2
  • 47
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
    • Jia Z, Barford D, Flint AJ, Tonks NK. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 1995; 268: 1754-1758.
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks, N.K.4
  • 48
    • 33646096207 scopus 로고    scopus 로고
    • PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects
    • Kontaridis MI, Swanson KD, David FS, Barford D, Neel BG. PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects. J Biol Chem 2006; 281: 6785-6792.
    • (2006) J Biol Chem , vol.281 , pp. 6785-6792
    • Kontaridis, M.I.1    Swanson, K.D.2    David, F.S.3    Barford, D.4    Neel, B.G.5
  • 49
    • 0027500821 scopus 로고
    • Expression, purification, and characterization of SH2-containing protein tyrosine phosphatase, SH-PTP2
    • Sugimoto S, Lechleider RJ, Shoelson SE, Neel BG, Walsh CT. Expression, purification, and characterization of SH2-containing protein tyrosine phosphatase, SH-PTP2. J Biol Chem 1993; 268: 22771-22776.
    • (1993) J Biol Chem , vol.268 , pp. 22771-22776
    • Sugimoto, S.1    Lechleider, R.J.2    Shoelson, S.E.3    Neel, B.G.4    Walsh, C.T.5
  • 50
    • 0032521428 scopus 로고    scopus 로고
    • Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2
    • Barford D, Neel BG. Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2. Structure 1998; 6: 249-254.
    • (1998) Structure , vol.6 , pp. 249-254
    • Barford, D.1    Neel, B.G.2
  • 51
    • 0030061843 scopus 로고    scopus 로고
    • Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1
    • Pei D, Wang J, Walsh CT. Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1. Proc Natl Acad Sci USA 1996; 93: 1141-1145.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1141-1145
    • Pei, D.1    Wang, J.2    Walsh, C.T.3
  • 52
    • 0035968279 scopus 로고    scopus 로고
    • Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP2
    • Cunnick JM, Mei L, Doupnik CA, Wu J. Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP2. J Biol Chem 2001; 276: 24380-24387.
    • (2001) J Biol Chem , vol.276 , pp. 24380-24387
    • Cunnick, J.M.1    Mei, L.2    Doupnik, C.A.3    Wu, J.4


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