메뉴 건너뛰기




Volumn 293, Issue 3, 1999, Pages 613-627

The variable region-1 from tissue-type plasminogen activator confers specificity for plasminogen activator inhibitor-1 to thrombin by facilitating catalysis: Release of a kinetic block by a heterologous protein surface loop

Author keywords

Acylation; Crystal structure; Serine protease; SERPIN; Suicide substrate mechanism

Indexed keywords

HIRUGEN; PLASMINOGEN ACTIVATOR INHIBITOR; PLASMINOGEN ACTIVATOR INHIBITOR 1; SERINE PROTEINASE; SUICIDE SUBSTRATE; THROMBIN;

EID: 0032739834     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3178     Document Type: Article
Times cited : (25)

References (42)
  • 1
    • 0027326308 scopus 로고
    • Immunologic evidence for insertion of the reactive-bond loop of antithrombin into the A beta-sheet of the inhibitor during trapping of target proteinases
    • Björk I., Nordling K., Olson S. T. Immunologic evidence for insertion of the reactive-bond loop of antithrombin into the A beta-sheet of the inhibitor during trapping of target proteinases. Biochemistry. 32:1993;6501-6505.
    • (1993) Biochemistry , vol.32 , pp. 6501-6505
    • Björk, I.1    Nordling, K.2    Olson, S.T.3
  • 2
    • 0030791531 scopus 로고    scopus 로고
    • Inactivation of thrombin by antithrombin is accompanied by inactivation of regulatory exosite I
    • Bock P. E., Olson S. T., Björk I. Inactivation of thrombin by antithrombin is accompanied by inactivation of regulatory exosite I. J. Biol. Chem. 272:1997;19837-19845.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19837-19845
    • Bock, P.E.1    Olson, S.T.2    Björk, I.3
  • 3
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human alpha-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W., Mayr I., Baumann U., Huber R., Stone S. R., Hofsteenge J. The refined 1.9 Å crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 8:1989;3467-3475.
    • (1989) EMBO J. , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 4
    • 0027050807 scopus 로고
    • The refined 1.9 Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode W., Turk D., Karshikov A. The refined 1.9 Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci. 1:1992;426-471.
    • (1992) Protein Sci. , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 8
    • 0018893682 scopus 로고
    • On the regulation and control of fibrinolysis. Edward Kowalski Memorial Lecture
    • Collen D. On the regulation and control of fibrinolysis. Edward Kowalski Memorial Lecture. Thromb. Haemost. 43:1980;77-89.
    • (1980) Thromb. Haemost. , vol.43 , pp. 77-89
    • Collen, D.1
  • 9
    • 0025347305 scopus 로고
    • Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties
    • Ehrlich H. J., Gebbink R. K., Keijer J., Linders M., Preissner K. T., Pannekoek H. Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties. J. Biol. Chem. 265:1990;13029-13035.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13029-13035
    • Ehrlich, H.J.1    Gebbink, R.K.2    Keijer, J.3    Linders, M.4    Preissner, K.T.5    Pannekoek, H.6
  • 10
    • 0026355181 scopus 로고
    • Thrombin neutralizes plasminogen activator inhibitor 1 (PAI-1) that is complexed with vitronectin in the endothelial cell matrix
    • Ehrlich H. J., Klein-Gebbink R., Preissner K. T., Keijer J., Esmon N., Mertens N., Pannekoek H. Thrombin neutralizes plasminogen activator inhibitor 1 (PAI-1) that is complexed with vitronectin in the endothelial cell matrix. J. Cell. Biol. 115:1991;1773-1781.
    • (1991) J. Cell. Biol. , vol.115 , pp. 1773-1781
    • Ehrlich, H.J.1    Klein-Gebbink, R.2    Preissner, K.T.3    Keijer, J.4    Esmon, N.5    Mertens, N.6    Pannekoek, H.7
  • 11
    • 0019957643 scopus 로고
    • Computer- generated models of blood coagulation factor Xa, factor IXa, and thrombin based upon structural homology with other serine proteases
    • Furie B., Bing D. H., Feldmann R. J., Robison D. J., Burnier J. P., Furie B. C. Computer- generated models of blood coagulation factor Xa, factor IXa, and thrombin based upon structural homology with other serine proteases. J. Biol. Chem. 257:1982;3875-3882.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3875-3882
    • Furie, B.1    Bing, D.H.2    Feldmann, R.J.3    Robison, D.J.4    Burnier, J.P.5    Furie, B.C.6
  • 12
    • 0027388955 scopus 로고
    • Thrombin-variable region 1 (VR1). Evidence for the dominant contribution of VR1 of serine proteases to their interaction with plasminogen activator inhibitor 1
    • Horrevoets A. J. G., Tans G., Smilde A. E., van Zonneveld A.-J., Pannekoek H. Thrombin-variable region 1 (VR1). Evidence for the dominant contribution of VR1 of serine proteases to their interaction with plasminogen activator inhibitor 1. J. Biol. Chem. 268:1993;779-782.
    • (1993) J. Biol. Chem. , vol.268 , pp. 779-782
    • Horrevoets, A.J.G.1    Tans, G.2    Smilde, A.E.3    Van Zonneveld, A.-J.4    Pannekoek, H.5
  • 13
    • 0031018008 scopus 로고    scopus 로고
    • Production and characterization of recombinant human plasminogen(S741C-fluorescein). A novel approach to study zymogen activation without generation of active protease
    • Horrevoets A. J. G., Pannekoek H., Nesheim M. E. Production and characterization of recombinant human plasminogen(S741C-fluorescein). A novel approach to study zymogen activation without generation of active protease. J. Biol. Chem. 272:1997;2176-2182.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2176-2182
    • Horrevoets, A.J.G.1    Pannekoek, H.2    Nesheim, M.E.3
  • 14
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones T. A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11:1978;268-272.
    • (1978) J. Appl. Crystallog. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 15
    • 0029665065 scopus 로고    scopus 로고
    • The 2.3 Å crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator
    • Lamba D., Bauer M., Huber R., Fischer S., Rudolph R., Kohnert U., Bode W. The 2.3 Å crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator. J. Mol. Biol. 258:1996;117-135.
    • (1996) J. Mol. Biol. , vol.258 , pp. 117-135
    • Lamba, D.1    Bauer, M.2    Huber, R.3    Fischer, S.4    Rudolph, R.5    Kohnert, U.6    Bode, W.7
  • 17
    • 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. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 18
    • 0025740508 scopus 로고
    • Thrombin Glu-39 restricts the P'3 specificity to nonacidfic residues
    • Le Bonniec B. F., MacGillivray R. T. A., Esmon C. T. Thrombin Glu-39 restricts the P'3 specificity to nonacidfic residues. J. Biol. Chem. 266:1991;13796-13803.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13796-13803
    • Le Bonniec, B.F.1    MacGillivray, R.T.A.2    Esmon, C.T.3
  • 19
    • 0002414103 scopus 로고
    • Molecular data processing
    • D. Moras, A. D. Podjarny, & J. C. Thierry. Oxford: Oxford University Press
    • Leslie A. G. W. Molecular data processing. Moras D., Podjarny A. D., Thierry J. C. Crystallographic Computing 5. 1991;50-61 Oxford University Press, Oxford.
    • (1991) Crystallographic Computing 5 , pp. 50-61
    • Leslie, A.G.W.1
  • 20
    • 0025797042 scopus 로고
    • On the reversible interaction of plasminogen activator inhibitor-1 with tissue-type plasminogen activator and with urokinase-type plasminogen activator
    • Lijnen H. R., van Hoef B., Collen D. On the reversible interaction of plasminogen activator inhibitor-1 with tissue-type plasminogen activator and with urokinase-type plasminogen activator. J. Biol. Chem. 266:1991;4041-4044.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4041-4044
    • Lijnen, H.R.1    Van Hoef, B.2    Collen, D.3
  • 21
    • 0023857685 scopus 로고
    • Interactions of tissue-type plasminogen activator with plasma inhibitors and their pharmacologic implications
    • Lucore C. L., Sobel B. E. Interactions of tissue-type plasminogen activator with plasma inhibitors and their pharmacologic implications. Circulation. 77:1988;660-669.
    • (1988) Circulation , vol.77 , pp. 660-669
    • Lucore, C.L.1    Sobel, B.E.2
  • 25
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum likelihood method
    • Murshudov G. N., Vagin A. A., Dodson E. J. Refinement of macromolecular structures by the maximum likelihood method. Acta Crystallog. sect. D. 53:1997;240-255.
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 26
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 27
    • 0022389299 scopus 로고
    • Heparin and ionic strength-dependent conversion of antithrombin III from an inhibitor to a substrate of alpha-thrombin
    • Olson S. T. Heparin and ionic strength-dependent conversion of antithrombin III from an inhibitor to a substrate of alpha-thrombin. J. Biol. Chem. 260:1985;10153-10160.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10153-10160
    • Olson, S.T.1
  • 28
    • 0022885017 scopus 로고
    • Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III
    • Olson S. T., Shore J. D. Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. J. Biol. Chem. 261:1986;13151-13159.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13151-13159
    • Olson, S.T.1    Shore, J.D.2
  • 29
    • 0029587003 scopus 로고
    • Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes
    • Olson S. T., Bock P. E., Kvassman J., Shore J. D., Lawrence D. A., Ginsburg D., Björk I. Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes. J. Biol. Chem. 270:1995;30007-30017.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30007-30017
    • Olson, S.T.1    Bock, P.E.2    Kvassman, J.3    Shore, J.D.4    Lawrence, D.A.5    Ginsburg, D.6    Björk, I.7
  • 30
    • 0025788321 scopus 로고
    • Mechanism of serpin action: Evidence that C1 inhibitor functions as a suicide substrate
    • Patston P. A., Gettins P., Beechem J. M., Schapira M. Mechanism of serpin action: evidence that C1 inhibitor functions as a suicide substrate. Biochemistry. 30:1991;8876-8882.
    • (1991) Biochemistry , vol.30 , pp. 8876-8882
    • Patston, P.A.1    Gettins, P.2    Beechem, J.M.3    Schapira, M.4
  • 31
    • 0025804196 scopus 로고
    • Positional effects of sulfation in hirudin and hirudin PA related anticoagulant peptides
    • Payne M. H., Krstenansky J. L., Yates M. T., Mao S. J. Positional effects of sulfation in hirudin and hirudin PA related anticoagulant peptides. J. Med. Chem. 34:1991;1184-1187.
    • (1991) J. Med. Chem. , vol.34 , pp. 1184-1187
    • Payne, M.H.1    Krstenansky, J.L.2    Yates, M.T.3    Mao, S.J.4
  • 32
    • 0030742394 scopus 로고    scopus 로고
    • Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA
    • Renatus M., Engh R. A., Stubbs M. T., Huber R., Fischer S., Kohnert U., Bode W. Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA. EMBO J. 16:1997a;4797-4805.
    • (1997) EMBO J. , vol.16 , pp. 4797-4805
    • Renatus, M.1    Engh, R.A.2    Stubbs, M.T.3    Huber, R.4    Fischer, S.5    Kohnert, U.6    Bode, W.7
  • 33
    • 0030875839 scopus 로고    scopus 로고
    • Structural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors
    • Renatus M., Bode W., Huber R., Stürzebecher J., Prasa D., Fischer S., Kohnert U., Stubbs M. T. Structural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors. J. Biol. Chem. 272:1997b;21713-21719.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21713-21719
    • Renatus, M.1    Bode, W.2    Huber, R.3    Stürzebecher, J.4    Prasa, D.5    Fischer, S.6    Kohnert, U.7    Stubbs, M.T.8
  • 34
    • 0032558382 scopus 로고    scopus 로고
    • Elucidation of the structural basis for the slow reactivity of thrombin with plasminogen activator inhibitor-1
    • Rezaie A. R. Elucidation of the structural basis for the slow reactivity of thrombin with plasminogen activator inhibitor-1. Biochemistry. 37:1998;13138-13142.
    • (1998) Biochemistry , vol.37 , pp. 13138-13142
    • Rezaie, A.R.1
  • 35
    • 0028912190 scopus 로고
    • A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism
    • Shore J. D., Day D. E., Francis-Chmura A. M., Verhamme I., Kvassman J., Lawrence D. A., Ginsburg D. A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism. J. Biol. Chem. 270:1995;5395-5398.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5395-5398
    • Shore, J.D.1    Day, D.E.2    Francis-Chmura, A.M.3    Verhamme, I.4    Kvassman, J.5    Lawrence, D.A.6    Ginsburg, D.7
  • 36
    • 0030952675 scopus 로고    scopus 로고
    • Introduction of an RRHR motif into chicken urokinase-type plasminogen activator (ch-uPA) confers sensitivity to plasminogen activator inhibitor (PAI)-1 and PAI-2 and allows ch-uPA-mediated extracellular matrix degradation to be controlled by PAI-1
    • Sipley J. D., Alexander D. S., Testa J. E., Quigley J. P. Introduction of an RRHR motif into chicken urokinase-type plasminogen activator (ch-uPA) confers sensitivity to plasminogen activator inhibitor (PAI)-1 and PAI-2 and allows ch-uPA-mediated extracellular matrix degradation to be controlled by PAI-1. Proc. Natl Acad. Sci. USA. 94:1997;2933-2938.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2933-2938
    • Sipley, J.D.1    Alexander, D.S.2    Testa, J.E.3    Quigley, J.P.4
  • 39
    • 0025840544 scopus 로고
    • Meizothrombin formation during factor Xa-catalyzed prothrombin activation. Formation in a purified system and in plasma
    • Tans G., Janssen-Claessen T., Hemker H. C., Zwaal R. F., Rosing J. Meizothrombin formation during factor Xa-catalyzed prothrombin activation. Formation in a purified system and in plasma. J. Biol. Chem. 266:1991;21864-21873.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21864-21873
    • Tans, G.1    Janssen-Claessen, T.2    Hemker, H.C.3    Zwaal, R.F.4    Rosing, J.5
  • 40
    • 0029986456 scopus 로고    scopus 로고
    • Selective screening of a large phage display library of plasminogen activator inhibitor 1 mutants to localize interaction sites with either thrombin or the variable region 1 of tissue-type plasminogen activator
    • van Meijer M., Roelofs Y., Neels J., Horrevoets A. J. G., van Zonneveld A.-J., Pannekoek H. Selective screening of a large phage display library of plasminogen activator inhibitor 1 mutants to localize interaction sites with either thrombin or the variable region 1 of tissue-type plasminogen activator. J. Biol. Chem. 271:1996;7423-7428.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7423-7428
    • Van Meijer, M.1    Roelofs, Y.2    Neels, J.3    Horrevoets, A.J.G.4    Van Zonneveld, A.-J.5    Pannekoek, H.6
  • 41
    • 0030954682 scopus 로고    scopus 로고
    • The suicide substrate reaction between plasminogen activator inhibitor 1 and thrombin is regulated by the cofactors vitronectin and heparin
    • van Meijer M., Smilde A. E., Tans G., Nesheim M. E., Pannekoek H., Horrevoets A. J. G. The suicide substrate reaction between plasminogen activator inhibitor 1 and thrombin is regulated by the cofactors vitronectin and heparin. Blood. 90:1997;1874-1882.
    • (1997) Blood , vol.90 , pp. 1874-1882
    • Van Meijer, M.1    Smilde, A.E.2    Tans, G.3    Nesheim, M.E.4    Pannekoek, H.5    Horrevoets, A.J.G.6
  • 42
    • 0029591826 scopus 로고
    • The inhibition mechanism of serpins. Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex
    • Wilczynska M., Fa M., Ohlsson P. I., Ny T. The inhibition mechanism of serpins. Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex. J. Biol. Chem. 270:1995;29652-29655.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29652-29655
    • Wilczynska, M.1    Fa, M.2    Ohlsson, P.I.3    Ny, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.