메뉴 건너뛰기




Volumn 71, Issue 5, 1996, Pages 2830-2839

Crystal structures of thrombin with thiazole-containing inhibitors: Probes of the S1' binding site

Author keywords

[No Author keywords available]

Indexed keywords

THROMBIN; THROMBIN INHIBITOR;

EID: 0029965611     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79479-1     Document Type: Article
Times cited : (56)

References (45)
  • 1
    • 0028084791 scopus 로고
    • Molecular recognition by thrombin. Role of the slow→fast transition, site-specific ion binding energetics and thermodynamic mapping of structural components
    • Ayala, Y., and E. DiCera. 1994. Molecular recognition by thrombin. Role of the slow→fast transition, site-specific ion binding energetics and thermodynamic mapping of structural components. J. Mol. Biol. 235: 733-746.
    • (1994) J. Mol. Biol. , vol.235 , pp. 733-746
    • Ayala, Y.1    Dicera, E.2
  • 2
    • 0025837452 scopus 로고
    • Crystallographic analysis at 3.0-Å resolution of the binding to human thrombin of four active site-directed inhibitors
    • Banner, D., and P. Hadvary, 1991. Crystallographic analysis at 3.0-Å resolution of the binding to human thrombin of four active site-directed inhibitors. J. Biol. Chem. 266:20085-20093.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20085-20093
    • Banner, D.1    Hadvary, P.2
  • 3
    • 0024578173 scopus 로고
    • Free energy via molecular simulation: Applications to chemical and biomolecular systems
    • Beveridge, D., and F. DiCapua. 1989. Free energy via molecular simulation: applications to chemical and biomolecular systems. Annu. Rev. Biophys. Biophys. Chem. 18:431-492.
    • (1989) Annu. Rev. Biophys. Biophys. Chem. , vol.18 , pp. 431-492
    • Beveridge, D.1    DiCapua, F.2
  • 4
    • 0014221653 scopus 로고
    • Structure of N-terminal fragments of fibrinogen and specificity of thrombin
    • Blomback, B., M. Blomback, B. Hessel, and S. Iwanaga. 1967. Structure of N-terminal fragments of fibrinogen and specificity of thrombin. Nature. 215:1445-1448.
    • (1967) Nature , vol.215 , pp. 1445-1448
    • Blomback, B.1    Blomback, M.2    Hessel, B.3    Iwanaga, S.4
  • 5
    • 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., D. Turk, and A. Karshikov. 1992. 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. 1:426-471.
    • (1992) Protein Sci. , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 6
    • 0025175641 scopus 로고
    • Geometry of binding of the benzamidine- and arginine-based inhibitors NAPAP and MQPA to human alpha-thrombin. X-ray crystallographic determination of the NAPAP-trypsin complex and modeling of NAPAP-thrombin and MQPA-thrombin
    • Bode, W., D. Turk, and J. Sturzebecher. 1990. Geometry of binding of the benzamidine- and arginine-based inhibitors NAPAP and MQPA to human alpha-thrombin. X-ray crystallographic determination of the NAPAP-trypsin complex and modeling of NAPAP-thrombin and MQPA-thrombin. Eur. J. Biochem. 193:175-182.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 175-182
    • Bode, W.1    Turk, D.2    Sturzebecher, J.3
  • 7
    • 0026465007 scopus 로고
    • Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the benzamidine- and arginine-based thrombin inhibitors NAPAP, 4-TAPAP, and MQPA: A starting point for improving antithrombotics
    • Brandstetter, H., D. Turk, H. W. Hoeffken, D. Grosse, J. Sturzebecher, P. D. Martin, B. F. P. Edwards, and W. Bode. 1992. Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the benzamidine- and arginine-based thrombin inhibitors NAPAP, 4-TAPAP, and MQPA: a starting point for improving antithrombotics. J. Mol. Biol. 226:1085-1099.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1085-1099
    • Brandstetter, H.1    Turk, D.2    Hoeffken, H.W.3    Grosse, D.4    Sturzebecher, J.5    Martin, P.D.6    Edwards, B.F.P.7    Bode, W.8
  • 8
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein stabilization
    • Burley, S. K., and G. A. Petsko. 1985. Aromatic-aromatic interaction: a mechanism of protein stabilization. Science. 229:23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 10
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie, E. W., K. Fujikawa, and W. Kisiel. 1991. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry. 30:10363-10370.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 12
    • 0026731584 scopus 로고
    • Synthesis of a homologous series of ketomethylene arginyl pseudodipeptides and applications to low molecular weight hirudin-like thrombin inhibitors
    • DiMaio, J., B. Gibbs, Y. Konishi, J. Lefebre, and D. Munn. 1992. Synthesis of a homologous series of ketomethylene arginyl pseudodipeptides and applications to low molecular weight hirudin-like thrombin inhibitors. J. Med. Chem. 35:3331-3341.
    • (1992) J. Med. Chem. , vol.35 , pp. 3331-3341
    • DiMaio, J.1    Gibbs, B.2    Konishi, Y.3    Lefebre, J.4    Munn, D.5
  • 13
    • 0026546559 scopus 로고
    • Design, synthesis, and kinetic evaluation of a unique class of elastase inhibitors, the peptidyl alpha-ketobenzoxazoles, and the X-ray crystal structure of the covalent complex between porcine pancreatic elastase and Ac-Ala-Pro-Val-2-benzoxazole
    • Edwards, P. D., E. F. Meyer, Jr., J. Vijayalakshmi, P. A. Tuthill, D. A. Andisik, B. Gomes, and A. Strimpler. 1992. Design, synthesis, and kinetic evaluation of a unique class of elastase inhibitors, the peptidyl alpha-ketobenzoxazoles, and the X-ray crystal structure of the covalent complex between porcine pancreatic elastase and Ac-Ala-Pro-Val-2-benzoxazole. J. Am. Chem. Soc. 114:1854-1863.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 1854-1863
    • Edwards, P.D.1    Meyer Jr., E.F.2    Vijayalakshmi, J.3    Tuthill, P.A.4    Andisik, D.A.5    Gomes, B.6    Strimpler, A.7
  • 14
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • Esmon, C. T. 1989. The roles of protein C and thrombomodulin in the regulation of blood coagulation. J. Biol. Chem. 264:4743-4746.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4743-4746
    • Esmon, C.T.1
  • 15
    • 0020063793 scopus 로고
    • Isolation of membrane-bound cofactor for thrombin-catalyzed activation of protein C
    • Esmon, N. L., W. G. Owen, and C. T. Esmon. 1982. Isolation of membrane-bound cofactor for thrombin-catalyzed activation of protein C. J. Biol. Chem. 257:859-864.
    • (1982) J. Biol. Chem. , vol.257 , pp. 859-864
    • Esmon, N.L.1    Owen, W.G.2    Esmon, C.T.3
  • 16
    • 0002301187 scopus 로고
    • Incorporation of fast Fourier transforms to speed restrained least-squares refinement of protein structures
    • Finzel, B. C. 1987. Incorporation of fast Fourier transforms to speed restrained least-squares refinement of protein structures. J. Appl. Crystallogr. 20:53-55.
    • (1987) J. Appl. Crystallogr. , vol.20 , pp. 53-55
    • Finzel, B.C.1
  • 18
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structure
    • Hendrickson, W. A. 1985. Stereochemically restrained refinement of macromolecular structure. Methods Enzymol. 115:252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 19
    • 0001008852 scopus 로고
    • Auto-indexing of oscillation images
    • Higashi, T. 1990. Auto-indexing of oscillation images. J. Appl. Crystallogr. 23:253-257.
    • (1990) J. Appl. Crystallogr. , vol.23 , pp. 253-257
    • Higashi, T.1
  • 21
    • 0018120365 scopus 로고
    • The mechanism of the fibrinogenthrombin reaction
    • Hogg, D. H., and B. Blomback. 1978. The mechanism of the fibrinogenthrombin reaction. Thromb. Res. 12:953-964.
    • (1978) Thromb. Res. , vol.12 , pp. 953-964
    • Hogg, D.H.1    Blomback, B.2
  • 23
    • 0026690665 scopus 로고
    • Cloned platelet thrombin receptor is necessary for thrombin-induced platelet activation
    • Hung, D. T., T. K. H. Vu, V. I. Wheaton, K. Ishii, and S. R. Coughlin. 1992. Cloned platelet thrombin receptor is necessary for thrombin-induced platelet activation. J. Clin. Invest. 89:1350-1353.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1350-1353
    • Hung, D.T.1    Vu, T.K.H.2    Wheaton, V.I.3    Ishii, K.4    Coughlin, S.R.5
  • 25
    • 0019230494 scopus 로고
    • Thrombin inhibitors. 2. Amide derivatives of N-alpha-substituted L-arginine
    • Kikumoto, R., Y. Tamao, K. Ohkubo, T. Tezuka, and S. Tonomura. 1980. Thrombin inhibitors. 2. Amide derivatives of N-alpha-substituted L-arginine. J. Med. Chem. 23:830-836.
    • (1980) J. Med. Chem. , vol.23 , pp. 830-836
    • Kikumoto, R.1    Tamao, Y.2    Ohkubo, K.3    Tezuka, T.4    Tonomura, S.5
  • 27
    • 0029879577 scopus 로고    scopus 로고
    • Synthesis, structure, and structure-activity relationships of divalent thrombin inhibitors containing an alpha-ketoamide transition state mimetic
    • Krishnan, R., A. Tulinsky, G. P. Vlasuk, D. Pearson, P. Vallar, P. Bergum, T. K. Brunck, and W. C. Ripka. 1996. Synthesis, structure, and structure-activity relationships of divalent thrombin inhibitors containing an alpha-ketoamide transition state mimetic. Protein Sci. 5:422-433.
    • (1996) Protein Sci. , vol.5 , pp. 422-433
    • Krishnan, R.1    Tulinsky, A.2    Vlasuk, G.P.3    Pearson, D.4    Vallar, P.5    Bergum, P.6    Brunck, T.K.7    Ripka, W.C.8
  • 28
    • 0020655601 scopus 로고
    • The action of thrombin on peptide p-nitroanilide substrates. Substrate selectivity and examination of hydrolysis under different reaction conditions
    • Lottenberg, R., J. A. Hall, M. Blinder, E. P. Binder, and C. M. Jackson. 1983. The action of thrombin on peptide p-nitroanilide substrates. Substrate selectivity and examination of hydrolysis under different reaction conditions. Biochim. Biophys. Acta. 742:539-557.
    • (1983) Biochim. Biophys. Acta. , vol.742 , pp. 539-557
    • Lottenberg, R.1    Hall, J.A.2    Blinder, M.3    Binder, E.P.4    Jackson, C.M.5
  • 29
    • 0020507373 scopus 로고
    • Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P10
    • Marsh, H. C., Y. C. Meinwald, T. W. Thannhauser, and H. A. Scheraga. 1983. Mechanism of action of thrombin on fibrinogen. Kinetic evidence for involvement of aspartic acid at position P10. Biochemistry. 22: 4170-4174.
    • (1983) Biochemistry , vol.22 , pp. 4170-4174
    • Marsh, H.C.1    Meinwald, Y.C.2    Thannhauser, T.W.3    Scheraga, H.A.4
  • 31
    • 0013531559 scopus 로고
    • Active site mimetic inhibition of thrombin
    • Mathews, I. I., and A. Tulinsky. 1995. Active site mimetic inhibition of thrombin. Acta Crystallogr. D51:550-559.
    • (1995) Acta Crystallogr. , vol.D51 , pp. 550-559
    • Mathews, I.I.1    Tulinsky, A.2
  • 32
    • 0018374004 scopus 로고
    • Interactions of a fluorescent active-site-directed inhibitor of thrombin: Dansylarginine N-(3-ethyl-1,5-pentanediyl)amide
    • Nesheim, M. E., F. G. Prendergast, and K. G. Mann. 1979. Interactions of a fluorescent active-site-directed inhibitor of thrombin: dansylarginine N-(3-ethyl-1,5-pentanediyl)amide. Biochemistry. 18:996-1003.
    • (1979) Biochemistry , vol.18 , pp. 996-1003
    • Nesheim, M.E.1    Prendergast, F.G.2    Mann, K.G.3
  • 33
  • 34
  • 36
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • Rydel, T. J., A. Tulinsky, W. Bode, and R. Huber. 1991. Refined structure of the hirudin-thrombin complex. J. Mol. Biol. 221:583-601.
    • (1991) J. Mol. Biol. , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 37
    • 0023657928 scopus 로고
    • The geometries of interacting arginine-carboxyls in proteins
    • Singh, J., J. M. Thornton, M. Snarey, and S. F. Campbell. 1987. The geometries of interacting arginine-carboxyls in proteins. FEBS Lett. 224:161-171.
    • (1987) FEBS Lett. , vol.224 , pp. 161-171
    • Singh, J.1    Thornton, J.M.2    Snarey, M.3    Campbell, S.F.4
  • 39
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • Stubbs, M. T., and W. Bode. 1993. A player of many parts: the spotlight falls on thrombin's structure. Thromb. Res. 69:1-58.
    • (1993) Thromb. Res. , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 41
    • 0027410184 scopus 로고
    • Active site and exosite binding of alpha-thrombin
    • Tulinsky, A., and X. Qiu. 1993. Active site and exosite binding of alpha-thrombin. Blood Coag. Fibrin. 4:305-312.
    • (1993) Blood Coag. Fibrin. , vol.4 , pp. 305-312
    • Tulinsky, A.1    Qiu, X.2
  • 42
    • 0025851272 scopus 로고
    • Geometry of binding of alpha-tosylated piperidines of m-amidino, p-amidino- and p-guanidino phenylalanine to thrombin and trypsin. X-ray crystal structures of their trypsin complexes and modeling of their thrombin complexes
    • Turk, D., J. Sturzebecher, and W. Bode. 1991. Geometry of binding of alpha-tosylated piperidines of m-amidino, p-amidino- and p-guanidino phenylalanine to thrombin and trypsin. X-ray crystal structures of their trypsin complexes and modeling of their thrombin complexes. FEBS Lett. 287:133-138.
    • (1991) FEBS Lett. , vol.287 , pp. 133-138
    • Turk, D.1    Sturzebecher, J.2    Bode, W.3
  • 43
    • 0028586082 scopus 로고
    • The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: Changes accompanying activation and exosite binding to thrombin
    • Vijayalakshmi, J., K. P. Padmanabhan, K. G. Mann, and A. Tulinsky. 1994. The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: changes accompanying activation and exosite binding to thrombin. Protein Sci. 3:2254-2271.
    • (1994) Protein Sci. , vol.3 , pp. 2254-2271
    • Vijayalakshmi, J.1    Padmanabhan, K.P.2    Mann, K.G.3    Tulinsky, A.4
  • 44
    • 0025951949 scopus 로고
    • Single amino acid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin
    • Wu, Q., J. P. Sheehan, M. Tsiang, S. R. Lentz, J. J. Birktoft, and J. E. Sadler. 1991. Single amino acid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin. Proc. Natl. Acad. Sci. USA. 88:6775-6779.
    • (1991) Proc. Natl. Acad. Sci. USA. , vol.88 , pp. 6775-6779
    • Wu, Q.1    Sheehan, J.P.2    Tsiang, M.3    Lentz, S.R.4    Birktoft, J.J.5    Sadler, J.E.6
  • 45
    • 0027487088 scopus 로고
    • Crystal structure of the complex of human alpha-thrombin and non-hydrolyzable bifunctional inhibitors, hirutonin-2 and hirutonin-6
    • Zdanov, A., S. Wu, J. DiMaio, Y. Konishi, Y. Li, X. Wu, B. F. P. Edwards, P. D. Martin, and M. Cygler. 1993. Crystal structure of the complex of human alpha-thrombin and non-hydrolyzable bifunctional inhibitors, hirutonin-2 and hirutonin-6. Proteins. 17:252-265.
    • (1993) Proteins , vol.17 , pp. 252-265
    • Zdanov, A.1    Wu, S.2    DiMaio, J.3    Konishi, Y.4    Li, Y.5    Wu, X.6    Edwards, B.F.P.7    Martin, P.D.8    Cygler, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.