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Volumn 7, Issue 2, 1999, Pages 111-118

The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion

Author keywords

Metastable state; Plasminogen activator inhibitor 1; Serpin; Structure based drug design

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 1; SERINE PROTEINASE INHIBITOR;

EID: 0033081498     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80018-5     Document Type: Article
Times cited : (164)

References (42)
  • 1
    • 0029153839 scopus 로고
    • Plasminogen activator inhibitor-1 (PAI-1) in plasma: Its role in thrombotic disease
    • 1. Wiman, B. (1995). Plasminogen activator inhibitor-1 (PAI-1) in plasma: its role in thrombotic disease. Thromb, Haem. 74, 71-76.
    • (1995) Thromb, Haem. , vol.74 , pp. 71-76
    • Wiman, B.1
  • 2
    • 0030469517 scopus 로고    scopus 로고
    • The fibrinolytic system in neoplasia
    • 2. Bell, W.R. (1996). The fibrinolytic system in neoplasia. Sem. Thromb. Hemost. 22, 459-478.
    • (1996) Sem. Thromb. Hemost. , vol.22 , pp. 459-478
    • Bell, W.R.1
  • 3
    • 0028824030 scopus 로고
    • Serpin-protease complexes are trapped as stable acyl-enzyme intermediates
    • 3. Lawrence, D.A., et al., & Shore, J.D. (1995). Serpin-protease complexes are trapped as stable acyl-enzyme intermediates. J. Biol. Chem. 270, 25309-25312.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25309-25312
    • Lawrence, D.A.1    Shore, J.D.2
  • 4
    • 0029591826 scopus 로고
    • The inhibition mechanism of serpins: Evidence that the mobile reactive center loop is cleaved in the native protease - Inhibitor complex
    • 4. Wilczynska, M., Fa, M., Ohlsson, P.-I. & Ny, T. (1995). The inhibition mechanism of serpins: evidence that the mobile reactive center loop is cleaved in the native protease - inhibitor complex. J. Biol. Chem. 270, 29652-29655.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29652-29655
    • Wilczynska, M.1    Fa, M.2    Ohlsson, P.-I.3    Ny, T.4
  • 5
    • 0021747157 scopus 로고
    • 1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • 1-proteinase inhibitor: crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177, 531 -556.
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-556
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 6
    • 0026546881 scopus 로고
    • Structural basis of latency in plasminogen activator inhibitor-1
    • 6. Mottonen, J., et al., & Goldsmith, E.J. (1992). Structural basis of latency in plasminogen activator inhibitor-1. Nature 370, 270-273.
    • (1992) Nature , vol.370 , pp. 270-273
    • Mottonen, J.1    Goldsmith, E.J.2
  • 7
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • 7. Carrell, R.W., Evans, D.L. & Stein, P.E. (1991). Mobile reactive centre of serpins and the control of thrombosis. Nature 353, 576-578.
    • (1991) Nature , vol.353 , pp. 576-578
    • Carrell, R.W.1    Evans, D.L.2    Stein, P.E.3
  • 9
    • 0032532347 scopus 로고    scopus 로고
    • Antithrombins wibble and wobble (T85M/K): Archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation
    • 9. Beauchamp, N.J., et al., & Carrell, R.W. (1998). Antithrombins wibble and wobble (T85M/K): archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation. Blood, 92, 2696-2706.
    • (1998) Blood , vol.92 , pp. 2696-2706
    • Beauchamp, N.J.1    Carrell, R.W.2
  • 10
    • 0023685082 scopus 로고
    • Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma: Identification as a multimeric form of S protein (vitronectin)
    • 10. Declerck, P.J., et al., & Collen, D. (1988). Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma: identification as a multimeric form of S protein (vitronectin). J. Biol. Chem. 263, 15454-15461.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15454-15461
    • Declerck, P.J.1    Collen, D.2
  • 11
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • 11. Berkenpas, M.B., Lawrence, D.A. & Ginsburg, D. (1995). Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO J. 14, 2969-2977.
    • (1995) EMBO J. , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 12
    • 0029157233 scopus 로고
    • Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1
    • 12. Aertgeerts, K., DeBondt, H.L., DeRanter, C.J. & Declerck, P.J. (1995). Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nat. Struct. Biol. 2, 891-897.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 891-897
    • Aertgeerts, K.1    DeBondt, H.L.2    DeRanter, C.J.3    Declerck, P.J.4
  • 13
    • 0032524769 scopus 로고    scopus 로고
    • Interfering with the inhibitory mechanism of serpins: Crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide
    • 13. Xue, Y., et al., & Deinum, J. (1998). Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure 6, 627-636.
    • (1998) Structure , vol.6 , pp. 627-636
    • Xue, Y.1    Deinum, J.2
  • 14
    • 0028407364 scopus 로고
    • Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
    • 14. Wei, A., Rubin, H., Cooperman, B.S. & Christianson, D.W. (1994). Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nat. Struct. Biol. 1, 251-258.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 251-258
    • Wei, A.1    Rubin, H.2    Cooperman, B.S.3    Christianson, D.W.4
  • 15
    • 0028367551 scopus 로고
    • The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions
    • 15. Schreuder, H.A., et al., & Hol, W.G.J. (1994). The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nat. Struct. Biol. 1, 48-54.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 48-54
    • Schreuder, H.A.1    Hol, W.G.J.2
  • 16
    • 0028773279 scopus 로고
    • Biological implications of a 3 Å structure of dimeric antithrombin
    • 16. Carrell, R.W., Stein, P.E., Fermi, G. & Wardell, M.R. (1994). Biological implications of a 3 Å structure of dimeric antithrombin. Structure 2, 257-270.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 18
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • 18. Stein, P.E. & Carrell, R.W. (1995). What do dysfunctional serpins tell us about molecular mobility and disease? Nat. Struct. Biol. 2, 96-113.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 20
    • 0028855465 scopus 로고
    • COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization
    • 20. Eldering, E., Verpy, E., Roem, D., Meo, T. & Tosi, M. (1995). COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization. J. Biol. Chem. 270, 2579-2587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2579-2587
    • Eldering, E.1    Verpy, E.2    Roem, D.3    Meo, T.4    Tosi, M.5
  • 21
    • 0030062157 scopus 로고    scopus 로고
    • The biostructural pathology of the serpins: Critical function of sheet opening mechanism
    • 21. Carrell, R.W. & Stein, P.E. (1996). The biostructural pathology of the serpins: critical function of sheet opening mechanism. Biol. Chem. Hoppe-Seyler 377, 1-17.
    • (1996) Biol. Chem. Hoppe-Seyler , vol.377 , pp. 1-17
    • Carrell, R.W.1    Stein, P.E.2
  • 22
    • 0029317438 scopus 로고
    • Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition
    • 22. Tucker, H.M., Mottonen, J., Goldsmith, E.J. & Gerard, R.D. (1995). Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition. War. Struct. Biol. 2, 442-445.
    • (1995) War. Struct. Biol. , vol.2 , pp. 442-445
    • Tucker, H.M.1    Mottonen, J.2    Goldsmith, E.J.3    Gerard, R.D.4
  • 23
    • 0030898213 scopus 로고    scopus 로고
    • Characterization of the binding of different conformational forms of plasminogen activator inhibitor-1 to vitronectin: Implications for the regulation of pericellular proteolysis
    • 23. Lawrence, D.A, et al., & Ginsburg, D. (1997). Characterization of the binding of different conformational forms of plasminogen activator inhibitor-1 to vitronectin: implications for the regulation of pericellular proteolysis. J. Biol. Chem. 272, 7676-7680.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7676-7680
    • Lawrence, D.A.1    Ginsburg, D.2
  • 24
    • 0032513248 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 contains a cryptic high affinity binding site for the low density lipoprotein receptor related protein
    • 24. Stefansson, S., et al., & Lawrence, D.A. (1998). Plasminogen activator inhibitor-1 contains a cryptic high affinity binding site for the low density lipoprotein receptor related protein. J. Biol. Chem. 273, 6358-6366.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6358-6366
    • Stefansson, S.1    Lawrence, D.A.2
  • 26
    • 0029816265 scopus 로고    scopus 로고
    • Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?
    • 26. Deng, G., Curriden, S.A., Wang, S., Rosenberg, S. & Loskutoff, D.J. (1996). Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release? J. Cell Biol. 134, 1563-1571.
    • (1996) J. Cell Biol. , vol.134 , pp. 1563-1571
    • Deng, G.1    Curriden, S.A.2    Wang, S.3    Rosenberg, S.4    Loskutoff, D.J.5
  • 27
    • 0030877824 scopus 로고    scopus 로고
    • Molecular crosstalk between adhesion receptors and proteolytic cascades in vascular remodelling
    • 27. Preissner, K.T., May, A.E., Wohn, K.D., Germer, M. & Kanse, S.M. (1997). Molecular crosstalk between adhesion receptors and proteolytic cascades in vascular remodelling. Thromb. Haem. 78, 88-95.
    • (1997) Thromb. Haem. , vol.78 , pp. 88-95
    • Preissner, K.T.1    May, A.E.2    Wohn, K.D.3    Germer, M.4    Kanse, S.M.5
  • 28
    • 0031902286 scopus 로고    scopus 로고
    • Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization
    • 28. Bajou, K., et al., & Foidart, J.M. (1998). Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization. Nat. Med. 4, 923-928.
    • (1998) Nat. Med. , vol.4 , pp. 923-928
    • Bajou, K.1    Foidart, J.M.2
  • 29
    • 0028339118 scopus 로고
    • Localization of vitronectin binding domain in plasminogen activator inhibitor-1
    • 29. Lawrence, D.A., Berkenpas, M.B., Palaniappan, S. & Ginsburg, D. (1994). Localization of vitronectin binding domain in plasminogen activator inhibitor-1. J. Biol. Chem. 269, 15223-15228.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15223-15228
    • Lawrence, D.A.1    Berkenpas, M.B.2    Palaniappan, S.3    Ginsburg, D.4
  • 30
    • 0039518548 scopus 로고    scopus 로고
    • Identification of the binding site for a low-molecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis
    • 30. Björquist, P., et al., & Deinum, J. (1998). Identification of the binding site for a low-molecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis. Biochemistry 37, 1227-1234.
    • (1998) Biochemistry , vol.37 , pp. 1227-1234
    • Björquist, P.1    Deinum, J.2
  • 33
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • 33. Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 35
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • 35. Brünger, A.T., et al., & Warren, G.L. (1998). Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 36
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • 36. Pannu, N.S. & Read, R.J. (1996). Improved structure refinement through maximum likelihood. Acta Crystallogr. A 52, 659-668.
    • (1996) Acta Crystallogr. A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 37
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures
    • 37. Jiang, J.S. & Brünger, A.T. (1994). Protein hydration observed by X-ray diffraction: solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol, 243, 100-115.
    • (1994) J. Mol. Biol , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brünger, A.T.2
  • 38
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • 38. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 39
    • 0001280470 scopus 로고
    • DEMON/ANGEL: A suite of programs to carry out density modification
    • 39. Vellieux, F.M.D.A.P., Hunt, J.F., Roy, S. & Read, R.J. (1995). DEMON/ANGEL: a suite of programs to carry out density modification. J. Appl. Crystallogr. 28, 347-351.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 347-351
    • Vellieux, F.M.D.A.P.1    Hunt, J.F.2    Roy, S.3    Read, R.J.4
  • 40
    • 0026244229 scopus 로고
    • MOLSCRIPT: Aprogram to produce both detailed and schematic plots of protein structure
    • 40. Kraulis, P.J. (1991). MOLSCRIPT: aprogram to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 0025742788 scopus 로고
    • Serpin tertiary structure transformation
    • 42. Stein, P. & Chothia, C. (1991 ). Serpin tertiary structure transformation. J. Mol. Biol. 221, 615-621.
    • (1991) J. Mol. Biol. , vol.221 , pp. 615-621
    • Stein, P.1    Chothia, C.2


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