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Volumn 82, Issue 7, 2014, Pages 1428-1443

Decoding the structural events in substrate-gating mechanism of eukaryotic prolyl oligopeptidase using normal mode analysis and molecular dynamics simulations

Author keywords

Domain interface; Enzyme mechanism; Serine proteases; Substrate entry

Indexed keywords

PROLYL ENDOPEPTIDASE; SERINE PROTEINASE;

EID: 84902109432     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24511     Document Type: Article
Times cited : (22)

References (55)
  • 2
    • 0036178438 scopus 로고    scopus 로고
    • The prolyl oligopeptidase family
    • Polgár L. The prolyl oligopeptidase family. Cell Mol Life Sci 2002;59:349-362.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 349-362
    • Polgár, L.1
  • 3
    • 0018085787 scopus 로고
    • Postproline cleaving enzyme: kinetic studies of size and stereospecificity of its active site
    • Walter R, Yoshimoto T. Postproline cleaving enzyme: kinetic studies of size and stereospecificity of its active site. Biochemistry 1978;17:4139-4144.
    • (1978) Biochemistry , vol.17 , pp. 4139-4144
    • Walter, R.1    Yoshimoto, T.2
  • 4
    • 3042766378 scopus 로고    scopus 로고
    • Evolutionary relationships of the prolyl oligopeptidase family enzymes
    • Venäläinen JI, Juvonen RO, Männistö PT. Evolutionary relationships of the prolyl oligopeptidase family enzymes. Eur J Biochem 2004;271:2705-2715.
    • (2004) Eur J Biochem , vol.271 , pp. 2705-2715
    • Venäläinen, J.I.1    Juvonen, R.O.2    Männistö, P.T.3
  • 6
    • 33845477051 scopus 로고    scopus 로고
    • Suggested functions for prolyl oligopeptidase: a puzzling paradox
    • Brandt I, Scharpé S, Lambeir A-M. Suggested functions for prolyl oligopeptidase: a puzzling paradox. Clin Chim Acta 2007;377:50-61.
    • (2007) Clin Chim Acta , vol.377 , pp. 50-61
    • Brandt, I.1    Scharpé, S.2    Lambeir, A.-M.3
  • 7
    • 13344282048 scopus 로고    scopus 로고
    • Prolyl oligopeptidase and bipolar disorder
    • Williams RSB. Prolyl oligopeptidase and bipolar disorder. Clin Neurosci Res 2004;4:233-242.
    • (2004) Clin Neurosci Res , vol.4 , pp. 233-242
    • Williams, R.S.B.1
  • 9
    • 0030822531 scopus 로고    scopus 로고
    • Prevention of amyloid-like deposition by a selective prolyl endopeptidase inhibitor, Y-29794, in senescence-accelerated mouse
    • Kato A, Fukunari A, Sakai Y, Nakajima T. Prevention of amyloid-like deposition by a selective prolyl endopeptidase inhibitor, Y-29794, in senescence-accelerated mouse. J Pharmacol Exp Ther 1997;283:328-335.
    • (1997) J Pharmacol Exp Ther , vol.283 , pp. 328-335
    • Kato, A.1    Fukunari, A.2    Sakai, Y.3    Nakajima, T.4
  • 11
    • 0028217535 scopus 로고
    • Lower serum prolyl endopeptidase enzyme activity in major depression: further evidence that peptidases play a role in the pathophysiology of depression
    • Maes M, Goossens F, Scharpé S, Meltzer HY, D'Hondt P, Cosyns P. Lower serum prolyl endopeptidase enzyme activity in major depression: further evidence that peptidases play a role in the pathophysiology of depression. Biol Psychiatry 1994;35:545-552.
    • (1994) Biol Psychiatry , vol.35 , pp. 545-552
    • Maes, M.1    Goossens, F.2    Scharpé, S.3    Meltzer, H.Y.4    D'Hondt, P.5    Cosyns, P.6
  • 12
    • 0036146663 scopus 로고    scopus 로고
    • Effects of the prolyl endopeptidase inhibitor S 17092 on cognitive deficits in chronic low dose MPTP-treated monkeys
    • Schneider JS, Giardiniere M, Morain P. Effects of the prolyl endopeptidase inhibitor S 17092 on cognitive deficits in chronic low dose MPTP-treated monkeys. Neuropsychopharmacology 2002;26:176-182.
    • (2002) Neuropsychopharmacology , vol.26 , pp. 176-182
    • Schneider, J.S.1    Giardiniere, M.2    Morain, P.3
  • 13
    • 0028802506 scopus 로고
    • Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: effects of antidepressants, mood stabilizers, and antipsychotic drugs
    • Maes M, Goossens F, Scharpé S, Calabrese J, Desnyder R, Meltzer HY. Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: effects of antidepressants, mood stabilizers, and antipsychotic drugs. Psychiatry Res 1995;58:217-225.
    • (1995) Psychiatry Res , vol.58 , pp. 217-225
    • Maes, M.1    Goossens, F.2    Scharpé, S.3    Calabrese, J.4    Desnyder, R.5    Meltzer, H.Y.6
  • 14
    • 0029061068 scopus 로고
    • Effect of a novel prolyl endopeptidase inhibitor, JTP-4819, on prolyl endopeptidase activity and substance P- and arginine-vasopressin-like immunoreactivity in the brains of aged rats
    • Toide K, Okamiya K, Iwamoto Y, Kato T. Effect of a novel prolyl endopeptidase inhibitor, JTP-4819, on prolyl endopeptidase activity and substance P- and arginine-vasopressin-like immunoreactivity in the brains of aged rats. J Neurochem 1995;65:234-240.
    • (1995) J Neurochem , vol.65 , pp. 234-240
    • Toide, K.1    Okamiya, K.2    Iwamoto, Y.3    Kato, T.4
  • 15
    • 0037342917 scopus 로고    scopus 로고
    • Effect of S 17092, a novel prolyl endopeptidase inhibitor, on substance P and alpha-melanocyte-stimulating hormone breakdown in the rat brain
    • Bellemère G, Morain P, Vaudry H, Jégou S. Effect of S 17092, a novel prolyl endopeptidase inhibitor, on substance P and alpha-melanocyte-stimulating hormone breakdown in the rat brain. J Neurochem 2003;84:919-929.
    • (2003) J Neurochem , vol.84 , pp. 919-929
    • Bellemère, G.1    Morain, P.2    Vaudry, H.3    Jégou, S.4
  • 16
    • 77952024780 scopus 로고    scopus 로고
    • Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors
    • Lawandi J, Gerber-Lemaire S, Juillerat-Jeanneret L, Moitessier N. Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors. J Med Chem 2010;53:3423-3438.
    • (2010) J Med Chem , vol.53 , pp. 3423-3438
    • Lawandi, J.1    Gerber-Lemaire, S.2    Juillerat-Jeanneret, L.3    Moitessier, N.4
  • 19
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis
    • Fülöp V, Böcskei Z, Polgár L. Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell 1998;94:161-170.
    • (1998) Cell , vol.94 , pp. 161-170
    • Fülöp, V.1    Böcskei, Z.2    Polgár, L.3
  • 20
    • 41949135032 scopus 로고    scopus 로고
    • Structure, function and biological relevance of prolyl oligopeptidase
    • Szeltner Z, Polgár L. Structure, function and biological relevance of prolyl oligopeptidase. Curr Protein Pept Sci 2008;9:96-107.
    • (2008) Curr Protein Pept Sci , vol.9 , pp. 96-107
    • Szeltner, Z.1    Polgár, L.2
  • 21
    • 33646869457 scopus 로고    scopus 로고
    • Structure-function properties of prolyl oligopeptidase family enzymes
    • Rea D, Fülöp V. Structure-function properties of prolyl oligopeptidase family enzymes. Cell Biochem Biophys 2006;44:349-365.
    • (2006) Cell Biochem Biophys , vol.44 , pp. 349-365
    • Rea, D.1    Fülöp, V.2
  • 22
    • 0034279642 scopus 로고    scopus 로고
    • Catalysis of serine oligopeptidases is controlled by a gating filter mechanism
    • Fülöp V, Szeltner Z, Polgár L. Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. EMBO Rep 2000;1:277-281.
    • (2000) EMBO Rep , vol.1 , pp. 277-281
    • Fülöp, V.1    Szeltner, Z.2    Polgár, L.3
  • 23
    • 2942741114 scopus 로고    scopus 로고
    • Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding
    • Szeltner Z, Rea D, Juhász T, Renner V, Fülöp V, Polgár L. Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding. J Mol Biol 2004;340:627-637.
    • (2004) J Mol Biol , vol.340 , pp. 627-637
    • Szeltner, Z.1    Rea, D.2    Juhász, T.3    Renner, V.4    Fülöp, V.5    Polgár, L.6
  • 24
    • 14844366112 scopus 로고    scopus 로고
    • Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity
    • Shan L, Mathews II, Khosla C. Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity. Proc Natl Acad Sci USA 2005;102:3599-3604.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3599-3604
    • Shan, L.1    Mathews, I.I.2    Khosla, C.3
  • 25
    • 77954367132 scopus 로고    scopus 로고
    • Induced-fit mechanism for prolyl endopeptidase
    • Li M, Chen C, Davies DR, Chiu TK. Induced-fit mechanism for prolyl endopeptidase. J Biol Chem 2010; 285:21487-21495.
    • (2010) J Biol Chem , vol.285 , pp. 21487-21495
    • Li, M.1    Chen, C.2    Davies, D.R.3    Chiu, T.K.4
  • 26
    • 23044435795 scopus 로고    scopus 로고
    • Flexibility of prolyl oligopeptidase: molecular dynamics and molecular framework analysis of the potential substrate pathways
    • Fuxreiter M, Magyar C, Juhász T, Szeltner Z, Polgár L, Simon I. Flexibility of prolyl oligopeptidase: molecular dynamics and molecular framework analysis of the potential substrate pathways. Proteins 2005; 60:504-512.
    • (2005) Proteins , vol.60 , pp. 504-512
    • Fuxreiter, M.1    Magyar, C.2    Juhász, T.3    Szeltner, Z.4    Polgár, L.5    Simon, I.6
  • 28
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis
    • Tirion.
    • Tirion. Large amplitude elastic motions in proteins from a single-parameter, atomic analysis. Phys Rev Lett 1996; 77:1905-1908.
    • (1996) Phys Rev Lett , vol.77 , pp. 1905-1908
  • 29
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • Web Server issue
    • Suhre K, Sanejouand Y-H. ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res 2004;32(Web Server issue):W610-W614.
    • (2004) Nucleic Acids Res , vol.32
    • Suhre, K.1    Sanejouand, Y.-H.2
  • 30
    • 0000216012 scopus 로고
    • Collective protein dynamics and nuclear spin relaxation
    • Brüschweiler R. Collective protein dynamics and nuclear spin relaxation. J Chem Phys 1995;102:3396-3403.
    • (1995) J Chem Phys , vol.102 , pp. 3396-3403
    • Brüschweiler, R.1
  • 31
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling 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
  • 32
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J. T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 2000; 302:205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 36
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins
    • Web Server issue
    • Wiederstein M, Sippl MJ. ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res 2007; 35(Web Server issue):W407-W410.
    • (2007) Nucleic Acids Res , vol.35
    • Wiederstein, M.1    Sippl, M.J.2
  • 37
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: assessment of protein models with three-dimensional profiles
    • Eisenberg D, Lüthy R, Bowie JU. VERIFY3D: assessment of protein models with three-dimensional profiles. Meth Enzymol 1997;277:396-404.
    • (1997) Meth Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Lüthy, R.2    Bowie, J.U.3
  • 38
    • 0027209697 scopus 로고
    • Multigrid solution of the nonlinear Poisson-Boltzmann equation and calculation of titration curves
    • Oberoi H, Allewell NM. Multigrid solution of the nonlinear Poisson-Boltzmann equation and calculation of titration curves. Biophys J 1993; 65:48-55.
    • (1993) Biophys J , vol.65 , pp. 48-55
    • Oberoi, H.1    Allewell, N.M.2
  • 40
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucl Acids Res 2004;32:1792-1797.
    • (2004) Nucl Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 41
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schüttelkopf AW, van Aalten DMF. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr D Biol Crystallogr 2004;60:1355-1363.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1355-1363
    • Schüttelkopf, A.W.1    van Aalten, D.M.F.2
  • 42
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM.Satisfying hydrogen bonding potential in proteins. J Mol Biol 1994;238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 43
    • 0037246863 scopus 로고    scopus 로고
    • MolMovDB: analysis and visualization of conformational change and structural flexibility
    • Echols N, Milburn D, Gerstein M. MolMovDB: analysis and visualization of conformational change and structural flexibility. Nucleic Acids Res 2003;31:478-482.
    • (2003) Nucleic Acids Res , vol.31 , pp. 478-482
    • Echols, N.1    Milburn, D.2    Gerstein, M.3
  • 44
    • 81755171903 scopus 로고    scopus 로고
    • Structural analysis of prolyl oligopeptidases using molecular docking and dynamics: insights into conformational changes and ligand binding
    • Kaushik S, Sowdhamini R. Structural analysis of prolyl oligopeptidases using molecular docking and dynamics: insights into conformational changes and ligand binding. PLoS One 2011;6:e26251.
    • (2011) PLoS One , vol.6
    • Kaushik, S.1    Sowdhamini, R.2
  • 45
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Web Server issue
    • Dundas J, Ouyang Z, Tseng J, Binkowski A, Turpaz Y, Liang J. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res 2006;34(Web Server issue):W116-W118.
    • (2006) Nucleic Acids Res , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 46
    • 69049084556 scopus 로고    scopus 로고
    • Breathing motions of a respiratory protein revealed by molecular dynamics simulations
    • Scorciapino MA, Robertazzi A, Casu M, Ruggerone P, Ceccarelli M. Breathing motions of a respiratory protein revealed by molecular dynamics simulations. J Am Chem Soc 2009;131:11825-11832.
    • (2009) J Am Chem Soc , vol.131 , pp. 11825-11832
    • Scorciapino, M.A.1    Robertazzi, A.2    Casu, M.3    Ruggerone, P.4    Ceccarelli, M.5
  • 47
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama F, Sanejouand Y-H. Conformational change of proteins arising from normal mode calculations. Protein Eng 2001;14:1-6.
    • (2001) Protein Eng , vol.14 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.-H.2
  • 49
    • 0042131827 scopus 로고    scopus 로고
    • Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
    • Thoma R, Löffler B, Stihle M, Huber W, Ruf A, Hennig M. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure 2003;11:947-959.
    • (2003) Structure , vol.11 , pp. 947-959
    • Thoma, R.1    Löffler, B.2    Stihle, M.3    Huber, W.4    Ruf, A.5    Hennig, M.6
  • 51
    • 33745024278 scopus 로고    scopus 로고
    • Symmetry, form, and shape: guiding principles for robustness in macromolecular machines
    • Tama F, Brooks CL. Symmetry, form, and shape: guiding principles for robustness in macromolecular machines. Annu Rev Biophys Biomol Struct 2006;35:115-133.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 115-133
    • Tama, F.1    Brooks, C.L.2
  • 52
    • 77952938726 scopus 로고    scopus 로고
    • Global dynamics of proteins: bridging between structure and function
    • Bahar I, Lezon TR, Yang L-W, Eyal E. Global dynamics of proteins: bridging between structure and function. Annu Rev Biophys 2010;39:23-42.
    • (2010) Annu Rev Biophys , vol.39 , pp. 23-42
    • Bahar, I.1    Lezon, T.R.2    Yang, L.-W.3    Eyal, E.4
  • 53
    • 79959236502 scopus 로고    scopus 로고
    • Use of umbrella sampling to calculate the entrance/exit pathway for Z-Pro-prolinal inhibitor in prolyl oligopeptidase
    • St-Pierre J-F, Karttunen M, Mousseau N, Róg T, Bunker A. Use of umbrella sampling to calculate the entrance/exit pathway for Z-Pro-prolinal inhibitor in prolyl oligopeptidase. J Chem Theory Comput 2011;7:1583-1594.
    • (2011) J Chem Theory Comput , vol.7 , pp. 1583-1594
    • St-Pierre, J.-F.1    Karttunen, M.2    Mousseau, N.3    Róg, T.4    Bunker, A.5
  • 54
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT. The PSIPRED protein structure prediction server. Bioinformatics 2000;16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3


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