메뉴 건너뛰기




Volumn 6, Issue 5, 1998, Pages 627-636

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

Author keywords

Complex; Crystal structure; Peptide; Plasminogen activator inhibitor type 1; Serpin

Indexed keywords

BINDING KINETICS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME INACTIVATION; ENZYME INHIBITOR; ENZYME SUBSTRATE; GLYCOSYLATION; IMMOBILIZED ENZYME; MOLECULAR WEIGHT; PLASMINOGEN; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SURFACE PLASMON RESONANCE TECHNIQUE;

EID: 0032524769     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00064-1     Document Type: Article
Times cited : (96)

References (39)
  • 2
    • 0028786263 scopus 로고
    • Structure of plasminogen activator inhibitor 1 (PAI-1) and its function in fibrinolysis - An update
    • van Meijer, M. & Pannekoek, H. (1995). Structure of plasminogen activator inhibitor 1 (PAI-1) and its function in fibrinolysis - an update. Fibrinolysis 9, 263-276.
    • (1995) Fibrinolysis , vol.9 , pp. 263-276
    • Van Meijer, M.1    Pannekoek, H.2
  • 3
    • 0030857519 scopus 로고    scopus 로고
    • Novel low molecular weight inhibitor of PAI-1 (XR5118) promotes endogenous fibrinolysis and reduces postthrombolysis thrombus growth in rabbits
    • Friederich, P.W., et al., & ten Cate, J.W. (1997). Novel low molecular weight inhibitor of PAI-1 (XR5118) promotes endogenous fibrinolysis and reduces postthrombolysis thrombus growth in rabbits. Circulation 96, 916-921.
    • (1997) Circulation , vol.96 , pp. 916-921
    • Friederich, P.W.1    Ten Cate, J.W.2
  • 4
    • 0028407364 scopus 로고
    • Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
    • 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
  • 5
    • 0028367551 scopus 로고
    • The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions
    • 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
  • 6
    • 0028773279 scopus 로고
    • Biological implications of a 3 a structure of dimeric antithrombin
    • Carrell, R.W., Stein, P.E., Fermi, G. & Wardell, M.R. (1994). Biological implications of a 3 A 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
  • 7
    • 0030062157 scopus 로고    scopus 로고
    • The biostructural pathology of the serpins: Critical function of sheet opening mechanism
    • 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
  • 8
    • 0040703822 scopus 로고    scopus 로고
    • Characterisation of the complex of plasminogen activator inhibitor type 1 with tissue-type plasminogen activator by mass spectrometry and size-exclusion chromatography
    • Strömqvist, M., et al., & Deinum, J. (1996). Characterisation of the complex of plasminogen activator inhibitor type 1 with tissue-type plasminogen activator by mass spectrometry and size-exclusion chromatography. Biochim. Biophys. Acta 1295, 103-109.
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 103-109
    • Strömqvist, M.1    Deinum, J.2
  • 9
    • 0030888853 scopus 로고    scopus 로고
    • The serpin-proteinase complex revealed
    • Lawrence, D.A. (1997). The serpin-proteinase complex revealed. Nat. Struct. Biol. 4, 339-341.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 339-341
    • Lawrence, D.A.1
  • 10
    • 0031036673 scopus 로고    scopus 로고
    • Major proteinase movement upon stable serpin-proteinase complex formation
    • Stratikos, E. & Gettins, P.G. (1997). Major proteinase movement upon stable serpin-proteinase complex formation. Proc. Natl Acad. Sci. USA 94, 453-458.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 453-458
    • Stratikos, E.1    Gettins, P.G.2
  • 11
    • 0031134386 scopus 로고    scopus 로고
    • Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins
    • Wilczynska, M., Fa, M., Karolin, J., Ohlsson, P.-I., Johansson, L.B-Ä. & Ny, T. (1997). Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins. Nat. Struct. Biol. 4, 354-356.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 354-356
    • Wilczynska, M.1    Fa, M.2    Karolin, J.3    Ohlsson, P.-I.4    Johansson, L.B.-Ä.5    Ny, T.6
  • 12
    • 0040115305 scopus 로고    scopus 로고
    • Epitopes on plasminogen activator inhibitor type-1 important for binding to tissue plasminogen activator
    • Björquist, P., Ehnebom, J., Inghardt, T. & Deinum, J. (1997). Epitopes on plasminogen activator inhibitor type-1 important for binding to tissue plasminogen activator. Biochim. Biophys. Acta 1341, 87-98.
    • (1997) Biochim. Biophys. Acta , vol.1341 , pp. 87-98
    • Björquist, P.1    Ehnebom, J.2    Inghardt, T.3    Deinum, J.4
  • 13
    • 0028064911 scopus 로고
    • Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop
    • Audenaert, A.-M., Knockaert, I., Collen, D. & Declerck, P.J. (1994). Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop. J. Biol. Chem. 269, 19559-19564.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19559-19564
    • Audenaert, A.-M.1    Knockaert, I.2    Collen, D.3    Declerck, P.J.4
  • 14
    • 0027945176 scopus 로고
    • Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition
    • Lawrence, D.A., Olson, S.T., Palaniappan, S. & Ginsburg, D. (1994). Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition. J. Biol. Chem. 269, 27657-27662.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27657-27662
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 15
    • 0029317438 scopus 로고
    • Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition
    • 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. Nat. Struct. Biol. 2, 442-445.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 442-445
    • Tucker, H.M.1    Mottonen, J.2    Goldsmith, E.J.3    Gerard, R.D.4
  • 16
    • 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. Identification of functional sites
    • 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. Identification of functional sites. Biochemistry 37, 1227-1234.
    • (1998) Biochemistry , vol.37 , pp. 1227-1234
    • Björquist, P.1    Deinum, J.2
  • 17
    • 0026546881 scopus 로고
    • Structural basis of latency in plasminogen activator inhibitor-1
    • Mottonen, J., et al., & Goldsmith, E.J. (1992). Structural basis of latency in plasminogen activator inhibitor-1. Nature 355, 270-273.
    • (1992) Nature , vol.355 , pp. 270-273
    • Mottonen, J.1    Goldsmith, E.J.2
  • 18
    • 0029161540 scopus 로고
    • Crystallization and X-ray diffraction data of the cleaved form of plasminogen activator inhibitor-1
    • Aertgeerts, K., De Bondt, H.L., De Ranter, C. & Declerck, P.J. (1995). Crystallization and X-ray diffraction data of the cleaved form of plasminogen activator inhibitor-1. Proteins 23, 118-121.
    • (1995) Proteins , vol.23 , pp. 118-121
    • Aertgeerts, K.1    De Bondt, H.L.2    De Ranter, C.3    Declerck, P.J.4
  • 19
    • 0029157233 scopus 로고
    • Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1
    • Aertgeerts, K., De Bondt, H.L., De Ranter, 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    De Bondt, H.L.2    De Ranter, C.J.3    Declerck, P.J.4
  • 20
    • 0025866580 scopus 로고
    • Substrate properties of C1 inhibitor Ma (alanine 434-glutamic acid). Genetic and Structural evidence suggesting that the P12-region contains critical determinants of serine protease inhibitor/substrate status
    • Skriver, K., et al., & Bock, S.C. (1991). Substrate properties of C1 inhibitor Ma (alanine 434-glutamic acid). Genetic and Structural evidence suggesting that the P12-region contains critical determinants of serine protease inhibitor/substrate status. J. Biol. Chem. 266, 9216-9221.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9216-9221
    • Skriver, K.1    Bock, S.C.2
  • 21
    • 0028824030 scopus 로고
    • Serpin-protease complexes are trapped as stable acyl-enzyme intermediates
    • Lawrence, D., 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.1    Shore, J.D.2
  • 23
    • 0026529071 scopus 로고
    • Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor
    • Björk, I., Ylinenjärvi, K., Olson, S.T. & Bock, P.E. (1992). Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor. J. Biol. Chem. 267, 1976-1982.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1976-1982
    • Björk, I.1    Ylinenjärvi, K.2    Olson, S.T.3    Bock, P.E.4
  • 24
    • 0028958184 scopus 로고
    • Peptide-mediated inactivation of recombinant and platelet plasminogen activator inhibitor-1 in vitro
    • Eitzman, D.T., et al., & Ginsburg, D. (1995). Peptide-mediated inactivation of recombinant and platelet plasminogen activator inhibitor-1 in vitro. J. Clin. Invest. 95, 2416-2420.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2416-2420
    • Eitzman, D.T.1    Ginsburg, D.2
  • 25
    • 0028832866 scopus 로고
    • The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into β-sheet A
    • Kvassman, J.-O., Lawrence, D.A. & Shore, J.D. (1995). The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into β-sheet A. J. Biol. Chem. 270, 27942-27947.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27942-27947
    • Kvassman, J.-O.1    Lawrence, D.A.2    Shore, J.D.3
  • 27
    • 0028596532 scopus 로고
    • Plasminogen activator inhibitor type-1 interacts exclusively with the proteinase domain of tissue plasminogen activator
    • Björquist, P., et al., & Deinum, J. (1994). Plasminogen activator inhibitor type-1 interacts exclusively with the proteinase domain of tissue plasminogen activator. Biochim. Biophys. Acta 1209, 191-202.
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 191-202
    • Björquist, P.1    Deinum, J.2
  • 28
    • 0022354051 scopus 로고
    • Increased plasma levels of a rapid inhibitor of tissue plasminogen activator in young survivors of myocardial infarction
    • Hamsten, A., Wiman, B., De Faire, U. & Blombäck, M. (1985). Increased plasma levels of a rapid inhibitor of tissue plasminogen activator in young survivors of myocardial infarction. New Engl. J. Med. 313, 1557-1563.
    • (1985) New Engl. J. Med. , vol.313 , pp. 1557-1563
    • Hamsten, A.1    Wiman, B.2    De Faire, U.3    Blombäck, M.4
  • 29
    • 0028485666 scopus 로고
    • Separation of active and inactive forms of recombinant human plasminogen activator inhibitor type 1 (PAI-1) expressed in Chinese hamster ovary cells: Comparison with native human PAI-1
    • Strömqvist, M., et al., & Hansson, L. (1994). Separation of active and inactive forms of recombinant human plasminogen activator inhibitor type 1 (PAI-1) expressed in Chinese hamster ovary cells: comparison with native human PAI-1. Prot. Exp. Pur. 5, 309-316.
    • (1994) Prot. Exp. Pur. , vol.5 , pp. 309-316
    • Strömqvist, M.1    Hansson, L.2
  • 32
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • Navaza, J. & Saludjian, P. (1997). AMoRe: an automated molecular replacement program package. Methods Enzymol. 276, 581-594.
    • (1997) Methods Enzymol. , vol.276 , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 33
    • 0011126038 scopus 로고
    • Daresbury Laboratory, Warrington, UK
    • The SERC (UK) Collaborative Computing Project No. 4. (1979). A Suite of Programs for Protein Crystallography. Daresbury Laboratory, Warrington, UK.
    • (1979) A Suite of Programs for Protein Crystallography
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, W.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, W.W.3    Kjeldgaard, M.4
  • 36
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 0031588685 scopus 로고    scopus 로고
    • The 2.6 a structure of antithrombin indicates a conformational change at the heparin binding site
    • Skinner, R., Abrahams, J.-P., Whisstock, J.C., Lesk, A.M., Carrell, R.W. & Wardell, M.R. (1997). The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site. J. Mol. Biol. 266, 601-609.
    • (1997) J. Mol. Biol. , vol.266 , pp. 601-609
    • Skinner, R.1    Abrahams, J.-P.2    Whisstock, J.C.3    Lesk, A.M.4    Carrell, R.W.5    Wardell, M.R.6
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of proteins
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Cryst. 24, 946-956.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-956
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.