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Volumn 6, Issue 7, 1997, Pages 1438-1448

The co-crystal structure of unliganded bovine α-thrombin and prethrombin-2: Movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand binding

Author keywords

Blood coagulation; Prethrombin 2; Protein structure; Serine proteases; X ray crystallography; thrombin

Indexed keywords

AMINO ACID; AMMONIUM SULFATE; APOENZYME; ARGININE; ENZYME INHIBITOR; ENZYME PRECURSOR; FIBRINOPEPTIDE A; GLUTAMIC ACID; ISOLEUCINE; MACROGOL; PRETHROMBIN 2; PROLINE; THROMBIN; TRYPSINOGEN; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 0030802519     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060708     Document Type: Article
Times cited : (37)

References (56)
  • 2
    • 0026606829 scopus 로고
    • Partial characterization of venebrate prothrombin cDNAs: Amplification and sequence analysis of the B chain of thrombin from nine different species
    • Banfield DK, MacGillivary RTA. 1992. Partial characterization of venebrate prothrombin cDNAs: Amplification and sequence analysis of the B chain of thrombin from nine different species. Proc Natl Acad Sci USA 89:2779-2783.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2779-2783
    • Banfield, D.K.1    MacGillivary, R.T.A.2
  • 5
    • 0017850232 scopus 로고
    • Crystal structure analysis and refinement of two variants of trigonal trypsinogen
    • Bode W, Huber R. 1978. Crystal structure analysis and refinement of two variants of trigonal trypsinogen. FEBS Lett 90:265-268.
    • (1978) FEBS Lett , vol.90 , pp. 265-268
    • Bode, W.1    Huber, R.2
  • 6
    • 0024431034 scopus 로고
    • The refined 1.9Å crystal structure of human alpha-thrombin: Interactions 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 SR, Hofsteenge J. 1989. The refined 1.9Å crystal structure of human alpha-thrombin: Interactions with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J 8:3467-3475.
    • (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
  • 7
    • 0027050807 scopus 로고
    • The refined 1.9Å crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active site geometry, and structure function relationships
    • Bode W, Turk D, Karshikov A. 1992. The refined 1.9Å crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-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
  • 8
    • 0026465007 scopus 로고
    • Refined 2.3Å X-ray crystal structure of bovine thrombin complexes formed with benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP. and MQPA
    • Brandstetter H, Turk D, Hoeffken HW, Grosse D, Stürzebecher J, Martin PD, Edwards BFP, Bode W. 1992. Refined 2.3Å X-ray crystal structure of bovine thrombin complexes formed with benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP. and MQPA. 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    Stürzebecher, J.5    Martin, P.D.6    Edwards, B.F.P.7    Bode, W.8
  • 9
    • 0024279342 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to a 2.8 Ä resolution structure of aspartate aminotransferase
    • Brünger AT. 1988. Crystallographic refinement by simulated annealing: Application to a 2.8 Ä resolution structure of aspartate aminotransferase. J Mol Biol 203:803-816.
    • (1988) J Mol Biol , vol.203 , pp. 803-816
    • Brünger, A.T.1
  • 11
    • 0028222277 scopus 로고
    • Expression of monocyte chemotactic protein-1 by monocytes and endothelial cells exposed to thrombin
    • Colotta F, Sciacca FL, Sironi M, Luini W, Rabiet MJ, Mantovani A. 1994. Expression of monocyte chemotactic protein-1 by monocytes and endothelial cells exposed to thrombin. Am J Pathol 144:975-985.
    • (1994) Am J Pathol , vol.144 , pp. 975-985
    • Colotta, F.1    Sciacca, F.L.2    Sironi, M.3    Luini, W.4    Rabiet, M.J.5    Mantovani, A.6
  • 12
    • 0026577704 scopus 로고
    • Characterization of a functional thrombin receptor: Issues and opportunities
    • Coughlin SR, Vu T-KH, Hung DT, Wheaton VI. 1992. Characterization of a functional thrombin receptor: Issues and opportunities. J Clin Invest 89:351-355.
    • (1992) J Clin Invest , vol.89 , pp. 351-355
    • Coughlin, S.R.1    Vu, T.-K.H.2    Hung, D.T.3    Wheaton, V.I.4
  • 13
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie EW, Fujikawa K, Kisiel W. 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
  • 14
    • 0025120271 scopus 로고
    • Use of fragments of hirudin to investigate the thrombin-hirudin interaction
    • Dennis S, Wallace A, Hofsteenge J, Stone SR. 1990. Use of fragments of hirudin to investigate the thrombin-hirudin interaction. Eur J Biochem 188:61-66.
    • (1990) Eur J Biochem , vol.188 , pp. 61-66
    • Dennis, S.1    Wallace, A.2    Hofsteenge, J.3    Stone, S.R.4
  • 16
    • 79952608525 scopus 로고
    • Accurate bond angle parameters for x-ray protein structure refinement
    • Engh RA, Huber R. 1991. Accurate bond angle parameters for x-ray protein structure refinement. Acta Crystallogr A47:392-400.
    • (1991) Acta Crystallogr , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 17
    • 0025291082 scopus 로고
    • Recombinant human protein C derivatives: Altered response to calcium resulting in enhanced activation by thrombin
    • Ehrlich HJ, Grinnell BW, Jaskunas SR, Esmon CT, Van SB, Bang NU. 1990. Recombinant human protein C derivatives: Altered response to calcium resulting in enhanced activation by thrombin. EMBO J 9:2367-2373.
    • (1990) EMBO J , vol.9 , pp. 2367-2373
    • Ehrlich, H.J.1    Grinnell, B.W.2    Jaskunas, S.R.3    Esmon, C.T.4    Van, S.B.5    Bang, N.U.6
  • 18
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • Esmon CT. 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
  • 19
    • 0023684353 scopus 로고
    • Regulation of thrombin generation and functions
    • Fenton JW II. 1988. Regulation of thrombin generation and functions. Semin Thromb Hemost 14:234-240.
    • (1988) Semin Thromb Hemost , vol.14 , pp. 234-240
    • Fenton II., J.W.1
  • 20
    • 0023770729 scopus 로고
    • Anion binding exosite of human α-thrombin and fibrin(ogen) recognition
    • Fenton JW II, Olson TA, Zahinski MP, Wilner GD. 1988. Anion binding exosite of human α-thrombin and fibrin(ogen) recognition. Biochemistry 27:7106-7112.
    • (1988) Biochemistry , vol.27 , pp. 7106-7112
    • Fenton II, J.W.1    Olson, T.A.2    Zahinski, M.P.3    Wilner, G.D.4
  • 21
    • 0014965896 scopus 로고
    • Chymotrypsinogen: 2.5Å crystal structure, comparison with α-chymotrypsin. and implications for zymogen activation
    • Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NH. 1970. Chymotrypsinogen: 2.5Å crystal structure, comparison with α-chymotrypsin. and implications for zymogen activation. Biochemistry 9:1997-2009.
    • (1970) Biochemistry , vol.9 , pp. 1997-2009
    • Freer, S.T.1    Kraut, J.2    Robertus, J.D.3    Wright, H.T.4    Xuong, N.H.5
  • 22
    • 0022924090 scopus 로고
    • Thrombin cleavage of extracellular matrix proteins: Bioregulatory functions of thrombin
    • Goldfarb RH, Liotta LA. 1986. Thrombin cleavage of extracellular matrix proteins: Bioregulatory functions of thrombin. Ann NY Acad Sci 485:288-292.
    • (1986) Ann NY Acad Sci , vol.485 , pp. 288-292
    • Goldfarb, R.H.1    Liotta, L.A.2
  • 24
    • 0028174260 scopus 로고
    • Glu192-Gln substitution in thrombin yields an enzyme that is effectively inhibited by bovine pancreatic trypsin inhibitor and tissue factor pathway inhibitor
    • Guinto ER, Ye J, LeBonniec BF, Esmon CT. 1994. Glu192-Gln substitution in thrombin yields an enzyme that is effectively inhibited by bovine pancreatic trypsin inhibitor and tissue factor pathway inhibitor. J Biol Chem 269:18395-18400.
    • (1994) J Biol Chem , vol.269 , pp. 18395-18400
    • Guinto, E.R.1    Ye, J.2    LeBonniec, B.F.3    Esmon, C.T.4
  • 25
    • 0000001574 scopus 로고
    • Thrombosis and fibrinolysis
    • Fuster V, Verstraete M, eds. Philadelphia, PA: W.B. Saunders
    • Harker, LA, Mann, KG. 1992. Thrombosis and fibrinolysis. In: Fuster V, Verstraete M, eds. In: Thrombosis in cardiovascular disorders. Philadelphia, PA: W.B. Saunders. pp 1-16.
    • (1992) Thrombosis in Cardiovascular Disorders , pp. 1-16
    • Harker, L.A.1    Mann, K.G.2
  • 26
    • 0025900393 scopus 로고
    • Allosteric changes in thrombin's activity produced by peptides corresponding to segments of natural inhibitors and substrates
    • Hortin GL, Trimpe BL. 1991. Allosteric changes in thrombin's activity produced by peptides corresponding to segments of natural inhibitors and substrates. J Biol Chem 266:6866-6871.
    • (1991) J Biol Chem , vol.266 , pp. 6866-6871
    • Hortin, G.L.1    Trimpe, B.L.2
  • 28
    • 0027724106 scopus 로고
    • Kinetics of factor Xa inhibition by tissue factor pathway inhibitor
    • Huang Z-F, Wun T-C, Broze GJJ. 1993. Kinetics of factor Xa inhibition by tissue factor pathway inhibitor. J Biol Chem 268:26950-26955.
    • (1993) J Biol Chem , vol.268 , pp. 26950-26955
    • Huang, Z.-F.1    Wun, T.-C.2    Broze, G.J.J.3
  • 29
    • 0004110665 scopus 로고
    • Correlation of crystal data and charge density with the reactivity and activity of molecules: Towards a description of elementary steps in enzyme reactions
    • Jeffrey, GA, Pinella, JF, eds. New York: Plenum Press
    • Klebe, G. 1991. Correlation of crystal data and charge density with the reactivity and activity of molecules: Towards a description of elementary steps in enzyme reactions. Jeffrey, GA, Pinella, JF, eds. In: The application of charge density research to chemistry and drug design. New York: Plenum Press, pp 287-318.
    • (1991) The Application of Charge Density Research to Chemistry and Drug Design , pp. 287-318
    • Klebe, G.1
  • 30
    • 0024264099 scopus 로고
    • Analysis of the secondary structure of hirudin and the mechanism of its interaction with thrombin
    • Konno S, Fenton JW II. Villanueva GB. 1988. Analysis of the secondary structure of hirudin and the mechanism of its interaction with thrombin. Arch Biochem Biophys 267:158-166.
    • (1988) Arch Biochem Biophys , vol.267 , pp. 158-166
    • Konno, S.1    Fenton II, J.W.2    Villanueva, G.B.3
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
  • 34
    • 0027177515 scopus 로고
    • The role of thrombin's Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin III, and the kunitz inhibitors
    • LeBonniec BF, Guinto ER, MacGillivary RTA, Stone SR, Esmon CT. 1993. The role of thrombin's Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin III, and the kunitz inhibitors. J Biol Chem 265:19055-19061.
    • (1993) J Biol Chem , vol.265 , pp. 19055-19061
    • LeBonniec, B.F.1    Guinto, E.R.2    MacGillivary, R.T.A.3    Stone, S.R.4    Esmon, C.T.5
  • 35
    • 0026003287 scopus 로고
    • The region of the thrombin receptor resembling hirudin binds to thrombin and alters enzyme specificity
    • Liu LW, Vu TKH, Esmon CT, Coughlin SR. 1991a. The region of the thrombin receptor resembling hirudin binds to thrombin and alters enzyme specificity. J Biol Chem 266:16977-16980.
    • (1991) J Biol Chem , vol.266 , pp. 16977-16980
    • Liu, L.W.1    Vu, T.K.H.2    Esmon, C.T.3    Coughlin, S.R.4
  • 36
    • 0026346977 scopus 로고
    • Proteolytic formation of either of the two prothrombin activation intermediates results in formation of a hirugen binding site
    • Liu LW, Ye J, Johnson AE, Esmon CT. 1991b. Proteolytic formation of either of the two prothrombin activation intermediates results in formation of a hirugen binding site. J Biol Chem 266:23632-23636.
    • (1991) J Biol Chem , vol.266 , pp. 23632-23636
    • Liu, L.W.1    Ye, J.2    Johnson, A.E.3    Esmon, C.T.4
  • 37
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determenationdes structures cristallines
    • Luzzati PV. 1952. Traitement statistique des erreurs dans la determenationdes structures cristallines. Acta Crystallogr 5:802-810.
    • (1952) Acta Crystallogr , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 38
  • 39
    • 0023781401 scopus 로고
    • Interaction of hirudin with thrombin: Identification of a minimal binding domain of hirudin that inhibits clotting activity
    • Mao SJT, Yates MT, Owen TJ, Krstenansky JL. 1988. Interaction of hirudin with thrombin: Identification of a minimal binding domain of hirudin that inhibits clotting activity. Biochemistry 27:8170-8173.
    • (1988) Biochemistry , vol.27 , pp. 8170-8173
    • Mao, S.J.T.1    Yates, M.T.2    Owen, T.J.3    Krstenansky, J.L.4
  • 40
    • 0343013561 scopus 로고
    • Purification and crystallization of bovine alpha-thrombin, inhibited with PMSF
    • Martin PD, Kumar VK, Tsemoglou D, Edwards BFP. 1983. Purification and crystallization of bovine alpha-thrombin, inhibited with PMSF. Fed Proc 42:1861-1861.
    • (1983) Fed Proc , vol.42 , pp. 1861-1861
    • Martin, P.D.1    Kumar, V.K.2    Tsemoglou, D.3    Edwards, B.F.P.4
  • 41
    • 0026657151 scopus 로고
    • The structure of residues 7-16 of the Aa-chain of human fibrinogen bound to bovine thrombin at 2.3 Å resolution
    • Martin PD, Robertson WD, Turk D, Huber R, Bode W, Edwards BFP. 1992. The structure of residues 7-16 of the Aa-chain of human fibrinogen bound to bovine thrombin at 2.3 Å resolution. J Biol Chem 267:7911-7920.
    • (1992) J Biol Chem , vol.267 , pp. 7911-7920
    • Martin, P.D.1    Robertson, W.D.2    Turk, D.3    Huber, R.4    Bode, W.5    Edwards, B.F.P.6
  • 42
    • 0029819059 scopus 로고    scopus 로고
    • Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen Aα: Geometry of the catalytic triad and interactions of the P1′, P2′, and P3′ substrate residues
    • Martin PD, Malkowski MG, DiMaio J, Konishi Y, Ni F, Edwards BFP. 1996. Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen Aα: Geometry of the catalytic triad and interactions of the P1′, P2′, and P3′ substrate residues. Biochemistry 35:13030-13039.
    • (1996) Biochemistry , vol.35 , pp. 13030-13039
    • Martin, P.D.1    Malkowski, M.G.2    DiMaio, J.3    Konishi, Y.4    Ni, F.5    Edwards, B.F.P.6
  • 44
    • 0024263049 scopus 로고
    • Meizothrombin, a major product of factor-Xa catalyzed prothrombin activation
    • Rosing J, Tans G. 1988. Meizothrombin, a major product of factor-Xa catalyzed prothrombin activation. Thromb Haemost 60:355-360.
    • (1988) Thromb Haemost , vol.60 , pp. 355-360
    • Rosing, J.1    Tans, G.2
  • 45
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossman MG, Blow DM. 1962. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallogr 15:24-31.
    • (1962) Acta Crystallogr , vol.15 , pp. 24-31
    • Rossman, M.G.1    Blow, D.M.2
  • 47
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin FAB McPC603: An X-ray diffraction study at 2.7 Å
    • Satow Y, Cohen GH, Padlan EA, Davies DR. 1986. Phosphocholine binding immunoglobulin FAB McPC603: An X-ray diffraction study at 2.7 Å. J Mol Biol 190:593-604.
    • (1986) J Mol Biol , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.R.4
  • 48
    • 0000359212 scopus 로고
    • Low temperature protein crystallography. Effect on flexibility, temperature factor, mosaic spread, extinction, and diffuse scattering in two examples: Bovine trypsinogen and Fc fragment
    • Singh TP, Bode W, Huber R. 1980. Low temperature protein crystallography. Effect on flexibility, temperature factor, mosaic spread, extinction, and diffuse scattering in two examples: Bovine trypsinogen and Fc fragment. Acta Crystallogr B36:621-627.
    • (1980) Acta Crystallogr , vol.B36 , pp. 621-627
    • Singh, T.P.1    Bode, W.2    Huber, R.3
  • 49
    • 0026548768 scopus 로고
    • The interaction of thrombin with fibrinogen: A structural basis for specificity
    • Stubbs MT, Bode W. 1992. The interaction of thrombin with fibrinogen: A structural basis for specificity. Eur J Biochem 206:187-195.
    • (1992) Eur J Biochem , vol.206 , pp. 187-195
    • Stubbs, M.T.1    Bode, W.2
  • 50
    • 0028586082 scopus 로고
    • The isomorphous structures of prethrombin-2, hirugen-, and PPACK-thromhin: Changes accompanying activation and exosite binding to thrombin
    • Vijayalakshmi J, Padmanabhan KG, Mann KG, Tulinsky A. 1994. The isomorphous structures of prethrombin-2, hirugen-, and PPACK-thromhin: 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.G.2    Mann, K.G.3    Tulinsky, A.4
  • 51
    • 0015387337 scopus 로고
    • Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges
    • Vincent J-P, Lazdunski M. 1972. Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges. Biochemistry 11:2967-2977.
    • (1972) Biochemistry , vol.11 , pp. 2967-2977
    • Vincent, J.-P.1    Lazdunski, M.2
  • 53
    • 0001631472 scopus 로고    scopus 로고
    • Structure of a bovine thrombin-hirudin51-65 complex determined by a combination of molecular replacement and graphics. Incorporation of known structural information in molecular replacement
    • Vitali J, Martin PD, Malkowski MG, Olsen CM, Johnson PH, Edwards BFP. 1996. Structure of a bovine thrombin-hirudin51-65 complex determined by a combination of molecular replacement and graphics. Incorporation of known structural information in molecular replacement. Acta Crystallogr D52:453-464.
    • (1996) Acta Crystallogr , vol.D52 , pp. 453-464
    • Vitali, J.1    Martin, P.D.2    Malkowski, M.G.3    Olsen, C.M.4    Johnson, P.H.5    Edwards, B.F.P.6
  • 54
    • 0001141858 scopus 로고
    • On the disordered activation domain in trypsinogen: Chemical labeling and low temperature crystallography
    • Walter J, Steigmann W, Singh TP. 1982. On the disordered activation domain in trypsinogen: Chemical labeling and low temperature crystallography. Acta Crystallogr B38:1462-1472.
    • (1982) Acta Crystallogr , vol.B38 , pp. 1462-1472
    • Walter, J.1    Steigmann, W.2    Singh, T.P.3
  • 55
    • 0021930156 scopus 로고
    • Bovine chymotrypsinogen A: X-ray crystal structure analysis and refinement of a new crystal form at 1.8Å resolution
    • Wang D, Bode W, Huber R. 1985. Bovine chymotrypsinogen A: X-ray crystal structure analysis and refinement of a new crystal form at 1.8Å resolution. J Mol Biol 185:595-624.
    • (1985) J Mol Biol , vol.185 , pp. 595-624
    • Wang, D.1    Bode, W.2    Huber, R.3


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