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Volumn 7, Issue 1, 1999, Pages 55-63

The 1.2 Å crystal structure of hirustasin reveals the intrinsic flexibility of a family of highly disulphide-bridged inhibitors

Author keywords

Ab initio; Anticoagulant; Conformational flexibility; Maximum likelihood; Serine protease inhibitors; SIRAS

Indexed keywords

ANTISTASIN; DISULFIDE; HIRUSTASIN; KALLIKREIN; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG; ANTICOAGULANT AGENT; BLOOD CLOTTING FACTOR 10A; HORMONE;

EID: 34548519838     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80009-4     Document Type: Article
Times cited : (35)

References (33)
  • 1
    • 0027972373 scopus 로고
    • Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis
    • Söllner, C., Mentele, R., Eckerskorn, C., Fritz, H. & Sommerhof, C.P. (1994). Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis. Eur. J. Biochem. 219, 937-943.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 937-943
    • Söllner, C.1    Mentele, R.2    Eckerskorn, C.3    Fritz, H.4    Sommerhof, C.P.5
  • 2
    • 0023189460 scopus 로고
    • Isolation and characterization of antistasin. An inhibitor of metastasis and coagulation
    • Tuszynski, G.P., Gasic, T.B. & Gasic, G.J. (1987). Isolation and characterization of antistasin. An inhibitor of metastasis and coagulation. J. Biol. Chem. 262, 9718-9723.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9718-9723
    • Tuszynski, G.P.1    Gasic, T.B.2    Gasic, G.J.3
  • 3
    • 0024321427 scopus 로고
    • Isolation and structural characterization of a potent inhibitor of coagulation factor Xa from the leech Haementeria ghilianii
    • Condra, C., Nutt, E., Petroski, C.J., Simpson, E., Friedman, P.A. & Jakobs, J.W. (1989). Isolation and structural characterization of a potent inhibitor of coagulation factor Xa from the leech Haementeria ghilianii. Thromb. Haemost. 61, 437-441.
    • (1989) Thromb. Haemost. , vol.61 , pp. 437-441
    • Condra, C.1    Nutt, E.2    Petroski, C.J.3    Simpson, E.4    Friedman, P.A.5    Jakobs, J.W.6
  • 4
    • 0029078878 scopus 로고
    • Isolation and characterisation of guamerin, a new human leukocyte elastase inhibitor from Hirudo nipponia
    • Jung, H.I., Kim, S.I., Ha, K.S., Joe, C.O. & Kang, K.W. (1995). Isolation and characterisation of guamerin, a new human leukocyte elastase inhibitor from Hirudo nipponia. J. Biol. Chem. 270, 13879-13884.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13879-13884
    • Jung, H.I.1    Kim, S.I.2    Ha, K.S.3    Joe, C.O.4    Kang, K.W.5
  • 5
    • 0031568813 scopus 로고    scopus 로고
    • A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex
    • Mini, P.R.E., et al., & Grütter, M.G. (1997). A new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex. Structure 5, 253-264.
    • (1997) Structure , vol.5 , pp. 253-264
    • Mini, P.R.E.1    Grütter, M.G.2
  • 6
    • 0023753262 scopus 로고
    • Purification and characterization of recombinant antistasin: A leech-derived inhibitor of coagulation factor Xa
    • Nutt, EM, Jain, D., Lenny, A.B., Schaffer, L, Siegl, P.K. & Dunwiddie, C.T. (1988). Purification and characterization of recombinant antistasin: A leech-derived inhibitor of coagulation factor Xa. J. Biol. Chem. 263, 10162-10167.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10162-10167
    • Nutt, E.M.1    Jain, D.2    Lenny, A.B.3    Schaffer, L.4    Siegl, P.K.5    Dunwiddie, C.T.6
  • 7
    • 0030852320 scopus 로고    scopus 로고
    • X-ray structure of antistasin at 1.9 Å resolution and its modelled complex with blood coagulation factor Xa
    • Lapatto, R., et al., & Dijkstra, B.W. (1997). X-ray structure of antistasin at 1.9 Å resolution and its modelled complex with blood coagulation factor Xa. EMBO J. 16, 5151-5161.
    • (1997) EMBO J. , vol.16 , pp. 5151-5161
    • Lapatto, R.1    Dijkstra, B.W.2
  • 8
    • 0027176270 scopus 로고
    • Anticoagulant potential of synthetic and recombinant inhibitors of factor Xa and thrombin in vitro
    • Hauptmann, J. & Kaiser, B. (1993). Anticoagulant potential of synthetic and recombinant inhibitors of factor Xa and thrombin in vitro. Thromb. Res. 71, 169-174.
    • (1993) Thromb. Res. , vol.71 , pp. 169-174
    • Hauptmann, J.1    Kaiser, B.2
  • 9
    • 0002272684 scopus 로고    scopus 로고
    • SHELX applications to macromolecules
    • (Fortier, S., ed), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Sheldrick, G.M. (1998). SHELX applications to macromolecules. In Direct Methods for Solving Macromolecular Structures. (Fortier, S., ed), pp. 401-441, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1998) Direct Methods for Solving Macromolecular Structures , pp. 401-441
    • Sheldrick, G.M.1
  • 10
    • 0027909076 scopus 로고
    • On the application of the minimal principle to solve unknown structures
    • Miller, R., DeTitta, G.T., Jones, R., Langs, D.A., Weeks, CM & Hauptman, H.A. (1993). On the application of the minimal principle to solve unknown structures. Science 259, 1430-1433.
    • (1993) Science , vol.259 , pp. 1430-1433
    • Miller, R.1    Detitta, G.T.2    Jones, R.3    Langs, D.A.4    Weeks, C.M.5    Hauptman, H.A.6
  • 11
    • 0028485498 scopus 로고
    • SnB: Crystal structure determination via shake-and-bake
    • Miller, R., Gallo, S.M., Khalak, H.G. & Weeks, C.M. (1994). SnB: Crystal structure determination via shake-and-bake. J. Appl. Cryst. 27, 613-621.
    • (1994) J. Appl. Cryst. , vol.27 , pp. 613-621
    • Miller, R.1    Gallo, S.M.2    Khalak, H.G.3    Weeks, C.M.4
  • 12
    • 0001053905 scopus 로고
    • Partial structural information combined with the tangent formula for noncentrosymmetric crystals
    • Karle, J. (1968). Partial structural information combined with the tangent formula for noncentrosymmetric crystals. Acta. Cryst. B 27, 182-186.
    • (1968) Acta. Cryst. B , vol.27 , pp. 182-186
    • Karle, J.1
  • 13
    • 37549022003 scopus 로고
    • Structure solution by iterative peaklist optimization and tangent expansion in space group P1
    • Sheldrick, G.M. & Gould, R.O. (1995). Structure solution by iterative peaklist optimization and tangent expansion in space group P1. Acta Cryst. B 51, 423-431.
    • (1995) Acta Cryst. B , vol.51 , pp. 423-431
    • Sheldrick, G.M.1    Gould, R.O.2
  • 14
    • 0002812783 scopus 로고
    • The application of direct methods and patterson interpretation to high-resolution native protein data
    • Sheldrick, G.M., Dauter, Z., Wilson, K.S., Hope, H. & Sieker, L.C. (1993). The application of direct methods and patterson interpretation to high-resolution native protein data. Acta Cryst. D 49, 18-23.
    • (1993) Acta Cryst. D , vol.49 , pp. 18-23
    • Sheldrick, G.M.1    Dauter, Z.2    Wilson, K.S.3    Hope, H.4    Sieker, L.C.5
  • 15
    • 85055704314 scopus 로고
    • Experiences with a new translation-function program
    • Fujinaga, M. & Read, R.J. (1987). Experiences with a new translation-function program. J. Appl. Cryst. 20, 517-521.
    • (1987) J. Appl. Cryst. , vol.20 , pp. 517-521
    • Fujinaga, M.1    Read, R.J.2
  • 16
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 17
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • De La Fortelle, E. & Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 19
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy-atom parameters
    • (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991). Maximum likelihood refinement of heavy-atom parameters. In Isomorphous Replacement and Anomalous Scattering. (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), pp. 80-85, SERC Daresbury Laboratory, Warrington, UK.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-85
    • Otwinowski, Z.1
  • 20
    • 0027465807 scopus 로고
    • Disulfide bonding patterns and protein topologies
    • Benham, C.J. & Jafri, S. (1993). Disulfide bonding patterns and protein topologies. Protein Sci. 2, 41-54.
    • (1993) Protein Sci. , vol.2 , pp. 41-54
    • Benham, C.J.1    Jafri, S.2
  • 21
    • 0020645978 scopus 로고
    • The X-ray structures of porcine pancreatic kallikrein and of its complex with bovine pancreatic trypsin inhibitor
    • Bode, W. & Chen, Z. (1983). The X-ray structures of porcine pancreatic kallikrein and of its complex with bovine pancreatic trypsin inhibitor. J. Mol. Biol. 164, 283-311.
    • (1983) J. Mol. Biol. , vol.164 , pp. 283-311
    • Bode, W.C.Z.1
  • 22
    • 0028260914 scopus 로고
    • Mutational analysis of antistasin, an inhibitor of blood coagulation factor Xa derived from the Mexican leech Haementeria officinalis
    • Theunissen, H.J., Dijkema, R., Swinkels, J.C., De Poorter, T.L., Vink, P.M. & Van Dinther, T.G. (1994). Mutational analysis of antistasin, an inhibitor of blood coagulation factor Xa derived from the Mexican leech Haementeria officinalis. Thromb. Res. 75, 41-50.
    • (1994) Thromb. Res. , vol.75 , pp. 41-50
    • Theunissen, H.J.1    Dijkema, R.2    Swinkels, J.C.3    De Poorter, T.L.4    Vink, P.M.5    Van Dinther, T.G.6
  • 23
    • 0031021543 scopus 로고    scopus 로고
    • Recombinant hirustasin: Production in yeast, crystallization, and interaction with serine proteases
    • Di Marco, S., et al., & Grütter, M.G. (1997). Recombinant hirustasin: Production in yeast, crystallization, and interaction with serine proteases. Protein Sci. 6, 109-118.
    • (1997) Protein Sci. , vol.6 , pp. 109-118
    • Di Marco, S.1    Grütter, M.G.2
  • 24
    • 85046526624 scopus 로고
    • Evaluation of single crystal X-ray diffraction from a position-sensitive detector
    • Kabsch, W. (1988). Evaluation of single crystal X-ray diffraction from a position-sensitive detector. J. Appl. Cryst. 21, 916-924.
    • (1988) J. Appl. Cryst. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 25
    • 85027633237 scopus 로고
    • Crystal orientation and X-ray pattern prediction for area-detector diffractometer systems in macromolecular crystallography
    • Messerschmidt, A. & Pflugrath, J.W. (1987). Crystal orientation and X-ray pattern prediction for area-detector diffractometer systems in macromolecular crystallography. J. Appl. Cryst. 20, 306-315.
    • (1987) J. Appl. Cryst. , vol.20 , pp. 306-315
    • Messerschmidt, A.1    Pflugrath, J.W.2
  • 26
  • 27
    • 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, S.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, S.W.3    Kjeldgaard, M.4
  • 28
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 29
    • 0016430638 scopus 로고
    • Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference fourier analysis
    • Moews, P.C. & Kretsinger, R.H. (1975). Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference fourier analysis. J. Mol. Biol. 91, 201-228.
    • (1975) J. Mol. Biol. , vol.91 , pp. 201-228
    • Moews, P.C.1    Kretsinger, R.H.2
  • 30
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0030729838 scopus 로고    scopus 로고
    • BOBSCRIPT
    • Esnouf, R.M. (1997). BOBSCRIPT. J. Mol. Graph. 15, 132-134.
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.