메뉴 건너뛰기




Volumn 35, Issue 2, 1999, Pages 218-234

Probing the activation of protein C by the thrombin-thrombomodulin complex using structural analysis, site-directed mutagenesis, and computer modeling

Author keywords

Activation rate; Protein C; Protein modeling; Thrombin; Thrombomodulin

Indexed keywords

MUTANT PROTEIN; PROTEIN C; RECOMBINANT PROTEIN; THROMBIN; THROMBOMODULIN;

EID: 0033135017     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19990501)35:2<218::AID-PROT8>3.0.CO;2-2     Document Type: Article
Times cited : (31)

References (85)
  • 2
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967;27:157-162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 3
  • 4
    • 0030850713 scopus 로고    scopus 로고
    • Resistance to activated protein C as risk factor for thrombosis: Molecular mechanisms, laboratory investigation, and clinical management
    • Dahlback B. Resistance to activated protein C as risk factor for thrombosis: molecular mechanisms, laboratory investigation, and clinical management. Semin Hernatol 1997;34:217-234.
    • (1997) Semin Hernatol , vol.34 , pp. 217-234
    • Dahlback, B.1
  • 6
    • 0017283234 scopus 로고
    • A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterization
    • Stenflo J. A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterization. J Biol Chem 1976;251:355-363.
    • (1976) J Biol Chem , vol.251 , pp. 355-363
    • Stenflo, J.1
  • 7
    • 0025056635 scopus 로고
    • Endoproteolytic processing of the dibasic cleavage site in the human protein C precursor in transfected mammalian cells: Effects of sequence alterations on efficiency of cleavage
    • Foster DC, Sprecher CA, Holly RD, Gambee JE, Walker KM, Kumar AA. Endoproteolytic processing of the dibasic cleavage site in the human protein C precursor in transfected mammalian cells: effects of sequence alterations on efficiency of cleavage. Biochemistry 1990;29:347-354.
    • (1990) Biochemistry , vol.29 , pp. 347-354
    • Foster, D.C.1    Sprecher, C.A.2    Holly, R.D.3    Gambee, J.E.4    Walker, K.M.5    Kumar, A.A.6
  • 8
    • 0021240173 scopus 로고
    • Characterization of a cDNA coding for human protein C
    • Foster D, Davie EW. Characterization of a cDNA coding for human protein C. Proc Natl Acad Sci USA 1984;81:4766-4770.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4766-4770
    • Foster, D.1    Davie, E.W.2
  • 9
    • 0000398357 scopus 로고    scopus 로고
    • Molecular model for the C-type lectin domain of human thrombomodulin
    • Villoutreix BO, Dahlbäck B. Molecular model for the C-type lectin domain of human thrombomodulin. J Mol Model 1998;4:310-322.
    • (1998) J Mol Model , vol.4 , pp. 310-322
    • Villoutreix, B.O.1    Dahlbäck, B.2
  • 10
    • 0022891349 scopus 로고
    • Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor
    • Jackman RW, Beeler DL, VanDeWater L, Rosenberg RD. Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor. Proc Natl Acad Sci USA 1986;83:8834-8838.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8834-8838
    • Jackman, R.W.1    Beeler, D.L.2    VanDeWater, L.3    Rosenberg, R.D.4
  • 12
    • 0023374585 scopus 로고
    • Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation
    • Suzuki K, Kusumoto H, Deyashiki Y, et al. Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation. EMBO J 1987;6:1891-1897.
    • (1987) EMBO J , vol.6 , pp. 1891-1897
    • Suzuki, K.1    Kusumoto, H.2    Deyashiki, Y.3
  • 13
    • 0025203764 scopus 로고
    • Further localization of binding sites for thrombin and protein C in human thrombomodulin
    • Hayashi T, Zushi M, Yamamoto S, Suzuki K. Further localization of binding sites for thrombin and protein C in human thrombomodulin. J Biol Chem 1990;265:20156-20159.
    • (1990) J Biol Chem , vol.265 , pp. 20156-20159
    • Hayashi, T.1    Zushi, M.2    Yamamoto, S.3    Suzuki, K.4
  • 14
    • 0026781041 scopus 로고
    • The fifth and sixth growth factor-like domains of thrombomodulin bind to the anion-binding exosite of thrombin and alter its specificity
    • Ye J, Liu LW, Esmon CT, Johnson AE. The fifth and sixth growth factor-like domains of thrombomodulin bind to the anion-binding exosite of thrombin and alter its specificity. J Biol Chem 1992;267: 11023-11028.
    • (1992) J Biol Chem , vol.267 , pp. 11023-11028
    • Ye, J.1    Liu, L.W.2    Esmon, C.T.3    Johnson, A.E.4
  • 15
    • 0026775230 scopus 로고
    • Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity
    • Tsiang M, Lentz SR, Sadler JE. Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity. J Biol Chem 1992;267:6164-6170.
    • (1992) J Biol Chem , vol.267 , pp. 6164-6170
    • Tsiang, M.1    Lentz, S.R.2    Sadler, J.E.3
  • 16
    • 0029958045 scopus 로고    scopus 로고
    • The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy
    • Weisel JW, Nagaswami C, Young TA, Light DR. The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy. J Biol Chem 1996;271:31485-31490.
    • (1996) J Biol Chem , vol.271 , pp. 31485-31490
    • Weisel, J.W.1    Nagaswami, C.2    Young, T.A.3    Light, D.R.4
  • 18
    • 0030843884 scopus 로고    scopus 로고
    • Thrombomodulin structure and function
    • Sadler JE. Thrombomodulin structure and function. Thromb Haemost 1997;78:392-395.
    • (1997) Thromb Haemost , vol.78 , pp. 392-395
    • Sadler, J.E.1
  • 19
    • 0027161205 scopus 로고
    • Molecular events that control the protein C anticoagulant pathway
    • Esmon CT. Molecular events that control the protein C anticoagulant pathway. Thromb Haemost 1993;70:29-35.
    • (1993) Thromb Haemost , vol.70 , pp. 29-35
    • Esmon, C.T.1
  • 22
    • 0028876697 scopus 로고
    • Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system
    • Healy AM, Rayburn HB, Rosenberg RD, Weiler H. Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system. Proc Natl Acad Sci USA 1995;92:850-854.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 850-854
    • Healy, A.M.1    Rayburn, H.B.2    Rosenberg, R.D.3    Weiler, H.4
  • 23
    • 0032080409 scopus 로고    scopus 로고
    • Target point mutation in thrombomodulin generates viable mice with a prethrombotic state
    • Weiler-Guettler PDC, Beeler DL, Healy AM, et al. Target point mutation in thrombomodulin generates viable mice with a prethrombotic state. J Clin Invest 1998;101:1983-1991.
    • (1998) J Clin Invest , vol.101 , pp. 1983-1991
    • Weiler-Guettler, P.D.C.1    Beeler, D.L.2    Healy, A.M.3
  • 24
    • 0027103736 scopus 로고
    • Oxidation of a specific methionine in thrombomodulin by activated neutrophil products blocks cofactor activity. A potential rapid mechanism for modulation of coagulation
    • Glaser CB, Morser J, Clarke JH, et al. Oxidation of a specific methionine in thrombomodulin by activated neutrophil products blocks cofactor activity. A potential rapid mechanism for modulation of coagulation. J Clin Invest 1992;90:2565-2573.
    • (1992) J Clin Invest , vol.90 , pp. 2565-2573
    • Glaser, C.B.1    Morser, J.2    Clarke, J.H.3
  • 25
    • 0027418066 scopus 로고
    • The short loop between epidermal growth factor-like domains 4 and 5 is critical for human thrombomodulin function
    • Clarke JH, Light DR, Blasko E, et al. The short loop between epidermal growth factor-like domains 4 and 5 is critical for human thrombomodulin function. J Biol Chem 1993;268:6309-6315.
    • (1993) J Biol Chem , vol.268 , pp. 6309-6315
    • Clarke, J.H.1    Light, D.R.2    Blasko, E.3
  • 26
    • 0029939761 scopus 로고    scopus 로고
    • Surface thrombomodulin modulates thrombin receptor responses on vascular smooth muscle cells
    • Grinnell BW, Berg DT. Surface thrombomodulin modulates thrombin receptor responses on vascular smooth muscle cells. Am J Physiol 1996;270:H603-H609.
    • (1996) Am J Physiol , vol.270
    • Grinnell, B.W.1    Berg, D.T.2
  • 27
    • 0031965910 scopus 로고    scopus 로고
    • Thrombomodulin modulates the mitogenic response to thrombin of human umbilical vein endothelial cells
    • Lafay RL, Le Bonniec BF, Lasne D, Aiach M, Rendu F. Thrombomodulin modulates the mitogenic response to thrombin of human umbilical vein endothelial cells. Thromb Haemost 1998;79:848-852.
    • (1998) Thromb Haemost , vol.79 , pp. 848-852
    • Lafay, R.L.1    Le Bonniec, B.F.2    Lasne, D.3    Aiach, M.4    Rendu, F.5
  • 28
    • 0025833619 scopus 로고
    • Protein s and C4b-binding protein: Components involved in the regulation of the protein C anticoagulant system
    • Dahlback B. Protein S and C4b-binding protein: components involved in the regulation of the protein C anticoagulant system. Thromb Haemost 1991;66:49-61.
    • (1991) Thromb Haemost , vol.66 , pp. 49-61
    • Dahlback, B.1
  • 29
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • Esmon CT. The roles of protein C and thrombomodulin in the regulation of blood coagulation. J Biol Chem 1989;264:4743-4746.
    • (1989) J Biol Chem , vol.264 , pp. 4743-4746
    • Esmon, C.T.1
  • 30
    • 0019861825 scopus 로고
    • Functional properties of an endothelial cell cofactor for thrombin-catalyzed activation of protein C
    • Owen WG, Esmon CT. Functional properties of an endothelial cell cofactor for thrombin-catalyzed activation of protein C. J Biol Chem 1981;256:5532-5535.
    • (1981) J Biol Chem , vol.256 , pp. 5532-5535
    • Owen, W.G.1    Esmon, C.T.2
  • 31
    • 0029827651 scopus 로고    scopus 로고
    • Effect of thrombomodulin on the molecular recognition and early events in thrombin-protein C interaction
    • De Cristofaro R. Effect of thrombomodulin on the molecular recognition and early events in thrombin-protein C interaction. Thromb Haemost 1996;76:556-560.
    • (1996) Thromb Haemost , vol.76 , pp. 556-560
    • De Cristofaro, R.1
  • 32
    • 0025923430 scopus 로고
    • Glu-192→Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin
    • Le Bonniec BF, Esmon CT. Glu-192→Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin. Proc Natl Acad Sci USA 1991;88:7371-7375.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7371-7375
    • Le Bonniec, B.F.1    Esmon, C.T.2
  • 33
    • 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, Yan SB, Bang NU. Recombinant human protein C derivatives: altered response to calcium resulting in enhanced activation by thrombin. EMBO J 1990;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    Yan, S.B.5    Bang, N.U.6
  • 34
    • 0025900393 scopus 로고
    • Allosteric changes in thrombin's activity produced by peptides corresponding to segments of natural inhibitors and substrates
    • Hortin GL, Trimpe BL. Allosteric changes in thrombin's activity produced by peptides corresponding to segments of natural inhibitors and substrates. J Biol Chem 1991;266:6866-6871.
    • (1991) J Biol Chem , vol.266 , pp. 6866-6871
    • Hortin, G.L.1    Trimpe, B.L.2
  • 35
    • 0028204534 scopus 로고
    • Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen
    • Fisher CL, Greengard JS, Griffin JH. Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen. Protein Sci 1994;3:588-599.
    • (1994) Protein Sci , vol.3 , pp. 588-599
    • Fisher, C.L.1    Greengard, J.S.2    Griffin, J.H.3
  • 36
    • 0028323166 scopus 로고
    • Structural basis for type I and type II deficiencies of antithrombotic plasma protein C: Patterns revealed by three-dimensional molecular modelling of mutations of the protease domain
    • Greengard JS, Fisher CL, Villoutreix B, Griffin JH. Structural basis for type I and type II deficiencies of antithrombotic plasma protein C: patterns revealed by three-dimensional molecular modelling of mutations of the protease domain. Proteins 1994;18: 367-380.
    • (1994) Proteins , vol.18 , pp. 367-380
    • Greengard, J.S.1    Fisher, C.L.2    Villoutreix, B.3    Griffin, J.H.4
  • 37
    • 0029787653 scopus 로고    scopus 로고
    • Mutation of protease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin
    • Gerlitz B, Grinnell BW. Mutation of protease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin. J Biol Chem 1996;271:22285-22288.
    • (1996) J Biol Chem , vol.271 , pp. 22285-22288
    • Gerlitz, B.1    Grinnell, B.W.2
  • 38
    • 0029983596 scopus 로고    scopus 로고
    • Structural investigation of the alpha-1-antichymotrypsin: Prostate-specific antigen complex by comparative model building
    • Villoutreix BO, Lilja H, Pettersson K, Lovgren T, Teleman O. Structural investigation of the alpha-1-antichymotrypsin: prostate-specific antigen complex by comparative model building. Protein Sci 1996;5:836-851.
    • (1996) Protein Sci , vol.5 , pp. 836-851
    • Villoutreix, B.O.1    Lilja, H.2    Pettersson, K.3    Lovgren, T.4    Teleman, O.5
  • 39
    • 0027983980 scopus 로고
    • Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin
    • Mathews II, Padmanabhan KP, Tulinksy A, Sadler JE. Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin. Biochemistry 1994;33:3547-13552.
    • (1994) Biochemistry , vol.33 , pp. 3547-13552
    • Mathews, I.I.1    Padmanabhan, K.P.2    Tulinksy, A.3    Sadler, J.E.4
  • 40
    • 0031864780 scopus 로고    scopus 로고
    • Rapid activation of protein C by factor Xa and thrombin in the presence of polyanionic compounds
    • Rezaie AR. Rapid activation of protein C by factor Xa and thrombin in the presence of polyanionic compounds. Blood 1998;91: 4572-4580.
    • (1998) Blood , vol.91 , pp. 4572-4580
    • Rezaie, A.R.1
  • 41
    • 0023654011 scopus 로고
    • Proteolytic formation and properties of functional domains of thrombomodulin
    • Kurosawa S, Galvin JB, Esmon NL, Esmon CT. Proteolytic formation and properties of functional domains of thrombomodulin. J Biol Chem 1987;262:2206-2212.
    • (1987) J Biol Chem , vol.262 , pp. 2206-2212
    • Kurosawa, S.1    Galvin, J.B.2    Esmon, N.L.3    Esmon, C.T.4
  • 42
    • 0028019030 scopus 로고
    • Modulation of glycoaminoglycan addition in naturally expressed and recombinant human thrombomodulin
    • Lin JH, McLean K, Morser J, Young T, Andrews WH, Light DR. Modulation of glycoaminoglycan addition in naturally expressed and recombinant human thrombomodulin. J Biol Chem 1994;269: 25021-25030.
    • (1994) J Biol Chem , vol.269 , pp. 25021-25030
    • Lin, J.H.1    McLean, K.2    Morser, J.3    Young, T.4    Andrews, W.H.5    Light, D.R.6
  • 43
    • 0031424043 scopus 로고    scopus 로고
    • Enhancing the activity of protein C by mutagenesis to improve the membrane-binding site: Studies related to proline-10
    • Shen L, Shah AM, Dahlback B, Nelsestuen GL. Enhancing the activity of protein C by mutagenesis to improve the membrane-binding site: studies related to proline-10. Biochemistry 1997;36: 16025-16031.
    • (1997) Biochemistry , vol.36 , pp. 16025-16031
    • Shen, L.1    Shah, A.M.2    Dahlback, B.3    Nelsestuen, G.L.4
  • 44
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey JH. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem 1981;117:307-310.
    • (1981) Anal Biochem , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 45
    • 0028982166 scopus 로고
    • The structure of a Ca(2+)-binding epidermal growth factor-like domain: Its role in protein-protein interactions
    • Rao Z, Handford P, Mayhew M, Knott V, Brownlee GG, Stuart D. The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions. Cell 1995;82:131-141.
    • (1995) Cell , vol.82 , pp. 131-141
    • Rao, Z.1    Handford, P.2    Mayhew, M.3    Knott, V.4    Brownlee, G.G.5    Stuart, D.6
  • 46
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder JW, Richards FM. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J Mol Biol 1987;193:775-791.
    • (1987) J Mol Biol , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 47
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • Jones TA, Thirup S. Using known substructures in protein model building and crystallography. EMBO J 1986;5:819-822.
    • (1986) EMBO J , vol.5 , pp. 819-822
    • Jones, T.A.1    Thirup, S.2
  • 48
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U, Sander C. Enlarged representative set of protein structures. Protein Sci 1994;3:522-524.
    • (1994) Protein Sci , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 49
    • 0023478807 scopus 로고
    • Predicting antibody hypervariable loop conformation. I. Ensembles of random conformations for ringlike structures
    • Shenkin PS, Yarmush DL, Fine RM, Wang HJ, Levinthal C. Predicting antibody hypervariable loop conformation. I. Ensembles of random conformations for ringlike structures. Biopolymers 1987;26:2053-2085.
    • (1987) Biopolymers , vol.26 , pp. 2053-2085
    • Shenkin, P.S.1    Yarmush, D.L.2    Fine, R.M.3    Wang, H.J.4    Levinthal, C.5
  • 50
    • 0030000090 scopus 로고    scopus 로고
    • Solution structure of a pair of calcium-binding epidermal growth factor-like domains: Implications for the Marfan syndrome and other genetic disorders
    • Downing AK, Knott V, Werner JM, Cardy CM, Campbell ID, Handford PA. Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders. Cell 1996;85:597-605.
    • (1996) Cell , vol.85 , pp. 597-605
    • Downing, A.K.1    Knott, V.2    Werner, J.M.3    Cardy, C.M.4    Campbell, I.D.5    Handford, P.A.6
  • 51
    • 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 SR, 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 1989;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
  • 52
    • 0029115958 scopus 로고
    • Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin
    • Meininger DP, Hunter MJ, Komives EA. Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin. Protein Sci 1995;4:1683-1695.
    • (1995) Protein Sci , vol.4 , pp. 1683-1695
    • Meininger, D.P.1    Hunter, M.J.2    Komives, E.A.3
  • 53
    • 0031558779 scopus 로고    scopus 로고
    • Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern
    • Sampoli-Benitez BA, Hunter MJ, Meininger DP, Komives EA. Structure of the fifth EGF-like domain of thrombomodulin: an EGF-like domain with a novel disulfide-bonding pattern. J Mol Biol 1997;273:913-926.
    • (1997) J Mol Biol , vol.273 , pp. 913-926
    • Sampoli-Benitez, B.A.1    Hunter, M.J.2    Meininger, D.P.3    Komives, E.A.4
  • 54
    • 0021930156 scopus 로고
    • Bovine chymotrypsinogen A. X-ray crystal structure analysis and refinement of a new crystal form at 1.8 Å resolution
    • Wang D, Bode W, Huber R. Bovine chymotrypsinogen A. X-ray crystal structure analysis and refinement of a new crystal form at 1.8 Å resolution. J Mol Biol 1985;185:595-624.
    • (1985) J Mol Biol , vol.185 , pp. 595-624
    • Wang, D.1    Bode, W.2    Huber, R.3
  • 55
    • 0031137254 scopus 로고    scopus 로고
    • A theoretical model for the Gla-TSR-EGF-1 region of the anticoagulant cofactor protein S: From structural pathology to species-specific cofactor activity
    • Villoutreix BO, Teleman O, Dahlbäck B. A theoretical model for the Gla-TSR-EGF-1 region of the anticoagulant cofactor protein S: from structural pathology to species-specific cofactor activity. J Comput Aided Mol Des 1997;11:293-304.
    • (1997) J Comput Aided Mol Des , vol.11 , pp. 293-304
    • Villoutreix, B.O.1    Teleman, O.2    Dahlbäck, B.3
  • 56
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • Banner DW, D'Arcy A, Chene C, et al. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature 1996;380:41-46.
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.W.1    D'Arcy, A.2    Chene, C.3
  • 57
    • 0026597973 scopus 로고
    • Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution
    • Frigerio F, Coda A, Pugliese L, et al. Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution. J Mol Biol 1992;225:107-123.
    • (1992) J Mol Biol , vol.225 , pp. 107-123
    • Frigerio, F.1    Coda, A.2    Pugliese, L.3
  • 58
    • 0029083552 scopus 로고
    • Tryptophans 231 and 234 in protein C report the Ca2+ -dependent conformational change required for activation by the thrombin-thrombomodulin complex
    • Rezaie AR, Esmon CT. Tryptophans 231 and 234 in protein C report the Ca2+ -dependent conformational change required for activation by the thrombin-thrombomodulin complex. Biochemistry 1995;34:12221-12226.
    • (1995) Biochemistry , vol.34 , pp. 12221-12226
    • Rezaie, A.R.1    Esmon, C.T.2
  • 61
    • 0030877442 scopus 로고    scopus 로고
    • Selective loss of fibrinogen clotting in a loop-less thrombin
    • Dang QD, Sabetta M, Di Cera E. Selective loss of fibrinogen clotting in a loop-less thrombin. J Biol Chem 1997;272:19649-19651.
    • (1997) J Biol Chem , vol.272 , pp. 19649-19651
    • Dang, Q.D.1    Sabetta, M.2    Di Cera, E.3
  • 62
    • 0029990916 scopus 로고    scopus 로고
    • The role of the insertion loop around tryptophan 148 in the activity of thrombin
    • Di Bella EE, Scheraga HA. The role of the insertion loop around tryptophan 148 in the activity of thrombin. Biochemistry 1996;35: 4427-4433.
    • (1996) Biochemistry , vol.35 , pp. 4427-4433
    • Di Bella, E.E.1    Scheraga, H.A.2
  • 63
    • 0026733611 scopus 로고
    • Interaction of thrombin des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C. Structural link between the autolysis loop and the Tyr-Pro-Pro-Trp insertion of thrombin
    • Le Bonniec BF, Guinto ER, Esmon CT. Interaction of thrombin des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C. Structural link between the autolysis loop and the Tyr-Pro-Pro-Trp insertion of thrombin. J Biol Chem 1992;267:19341-19348.
    • (1992) J Biol Chem , vol.267 , pp. 19341-19348
    • Le Bonniec, B.F.1    Guinto, E.R.2    Esmon, C.T.3
  • 64
    • 0027177515 scopus 로고
    • The role of thrombin's Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin and the Kunitz inhibitors
    • Le Bonniec BF, Guinto ER, MacGillivray RTA, Stone SR, Esmon CT. The role of thrombin's Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin and the Kunitz inhibitors. J Biol Chem 1993;268:19055-19061.
    • (1993) J Biol Chem , vol.268 , pp. 19055-19061
    • Le Bonniec, B.F.1    Guinto, E.R.2    MacGillivray, R.T.A.3    Stone, S.R.4    Esmon, C.T.5
  • 65
    • 0026506310 scopus 로고
    • Recombinant human thrombomodulin. Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain
    • Parkinson JF, Vlahos C J, Yan SC, Bang NU. Recombinant human thrombomodulin. Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain. Biochem J 1992;283:151-157.
    • (1992) Biochem J , vol.283 , pp. 151-157
    • Parkinson, J.F.1    Vlahos, C.J.2    Yan, S.C.3    Bang, N.U.4
  • 66
    • 0027411150 scopus 로고
    • Alanine-scanning mutagenesis of the epidermal growth factor-like domains of human thrombomodulin identifies critical residues for its cofactor activity
    • Nagashima M, Lundh E, Leonard JC, Morser J, Parkinson JF. Alanine-scanning mutagenesis of the epidermal growth factor-like domains of human thrombomodulin identifies critical residues for its cofactor activity. J Biol Chem 1993;268:2888-2892.
    • (1993) J Biol Chem , vol.268 , pp. 2888-2892
    • Nagashima, M.1    Lundh, E.2    Leonard, J.C.3    Morser, J.4    Parkinson, J.F.5
  • 67
    • 0028804818 scopus 로고
    • The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin
    • Adler M, Seto MH, Nitecki DE, Lin JH, Light DR, Morser J. The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin. J Biol Chem 1995;270:23366-23372.
    • (1995) J Biol Chem , vol.270 , pp. 23366-23372
    • Adler, M.1    Seto, M.H.2    Nitecki, D.E.3    Lin, J.H.4    Light, D.R.5    Morser, J.6
  • 68
    • 0032560618 scopus 로고    scopus 로고
    • Calcium binding properties of an epidermal growth factor-like domain from human thrombomodulin
    • Tolkatchev D, Ni F. Calcium binding properties of an epidermal growth factor-like domain from human thrombomodulin. Biochemistry 1998;37:9091-9100.
    • (1998) Biochemistry , vol.37 , pp. 9091-9100
    • Tolkatchev, D.1    Ni, F.2
  • 69
    • 0030742896 scopus 로고    scopus 로고
    • Thrombin, thrombomodulin and TAFi in the molecular link between coagulation and fibrinolysis
    • Nesheim M, Wang W, Boffa M, Nagashima M, Morser J, Bajzar L. Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis. Thromb Haemost 1997;78: 386-391.
    • (1997) Thromb Haemost , vol.78 , pp. 386-391
    • Nesheim, M.1    Wang, W.2    Boffa, M.3    Nagashima, M.4    Morser, J.5    Bajzar, L.6
  • 70
    • 0032524918 scopus 로고    scopus 로고
    • Activation of thrombin-activable fibronolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C
    • Kokame K, Zheng X, Sadler JE. Activation of thrombin-activable fibronolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C. J Biol Chem 1998;273:12135-12139.
    • (1998) J Biol Chem , vol.273 , pp. 12135-12139
    • Kokame, K.1    Zheng, X.2    Sadler, J.E.3
  • 71
    • 0028801352 scopus 로고
    • X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B
    • Brandstetter H, Bauer M, Huber R, Lollar P, Bode W. X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B. Proc Natl Acad Sci USA 1995;92:9796-800.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9796-9800
    • Brandstetter, H.1    Bauer, M.2    Huber, R.3    Lollar, P.4    Bode, W.5
  • 72
    • 0030770425 scopus 로고    scopus 로고
    • Protein s alters the active site location of activated protein C above the membrane surface. A fluorescence resonance energy transfer study of topography
    • Yegneswaran S, Wood GM, Esmon CT, Johnson AE. Protein S alters the active site location of activated protein C above the membrane surface. A fluorescence resonance energy transfer study of topography. J Biol Chem 1997;272:25013-25021.
    • (1997) J Biol Chem , vol.272 , pp. 25013-25021
    • Yegneswaran, S.1    Wood, G.M.2    Esmon, C.T.3    Johnson, A.E.4
  • 73
    • 0032474441 scopus 로고    scopus 로고
    • The solution structure of human coagulation factor VIIa in its complex with tissue factor is similar to free factor VIIa: A study of a heterodimeric receptor-ligand complex by X-ray and neutron scattering and computational modeling
    • Ashton AW, Boehm MK, Johnson DJD, Kemball-Cook G, Perkins SJ. The solution structure of human coagulation factor VIIa in its complex with tissue factor is similar to free factor VIIa: a study of a heterodimeric receptor-ligand complex by X-ray and neutron scattering and computational modeling. Biochemistry 1998;37: 8208-8217.
    • (1998) Biochemistry , vol.37 , pp. 8208-8217
    • Ashton, A.W.1    Boehm, M.K.2    Johnson, D.J.D.3    Kemball-Cook, G.4    Perkins, S.J.5
  • 74
    • 0028299524 scopus 로고
    • Proline at the P2 position in protein C is important for calcium-mediated regulation of protein C activation and secretion
    • Rezaie AR, Esmon CT. Proline at the P2 position in protein C is important for calcium-mediated regulation of protein C activation and secretion. Blood 1994;83:2526-2531.
    • (1994) Blood , vol.83 , pp. 2526-2531
    • Rezaie, A.R.1    Esmon, C.T.2
  • 75
    • 0027053116 scopus 로고
    • Electrostatic interactions in the association of proteins: An analysis of the thrombinhirudin complex
    • Karshikov A, Bode W, Tulinsky A, Stone SR. Electrostatic interactions in the association of proteins: an analysis of the thrombinhirudin complex. Protein Sci 1992;1:727-735.
    • (1992) Protein Sci , vol.1 , pp. 727-735
    • Karshikov, A.1    Bode, W.2    Tulinsky, A.3    Stone, S.R.4
  • 76
    • 0029000452 scopus 로고
    • Amino acids 225-235 of the protein C serine protease domain are important for the interaction with the thrombin-thrombomodulin complex
    • Vincenot A, Gaussem P, Pittet JL, Debost S, Aiach M. Amino acids 225-235 of the protein C serine protease domain are important for the interaction with the thrombin-thrombomodulin complex. FEBS Lett 1995;367:153-157.
    • (1995) FEBS Lett , vol.367 , pp. 153-157
    • Vincenot, A.1    Gaussem, P.2    Pittet, J.L.3    Debost, S.4    Aiach, M.5
  • 77
    • 0030959346 scopus 로고    scopus 로고
    • The thrombin E192Q-BPTI complex reveals gross structural rearrangements: Implications for the interaction with antithrombin and thrombomodulin
    • van de Locht A, Bode W, Huber R, Le Bonniec BF, Stone SR, Esmon CT, Stubbs MT. The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin. EMBO J 1997;16:2977-2984.
    • (1997) EMBO J , vol.16 , pp. 2977-2984
    • Van De Locht, A.1    Bode, W.2    Huber, R.3    Le Bonniec, B.F.4    Stone, S.R.5    Esmon, C.T.6    Stubbs, M.T.7
  • 78
    • 0026610497 scopus 로고
    • Ca2+ dependence of the interactions between protein C, thrombin, and the elastase fragment of thrombomodulin. Analysis by ultracentrifugation
    • Olsen PH, Esmon NL, Esmon CT, Laue TM. Ca2+ dependence of the interactions between protein C, thrombin, and the elastase fragment of thrombomodulin. Analysis by ultracentrifugation. Biochemistry 1992;31:746-754.
    • (1992) Biochemistry , vol.31 , pp. 746-754
    • Olsen, P.H.1    Esmon, N.L.2    Esmon, C.T.3    Laue, T.M.4
  • 79
    • 0022531794 scopus 로고
    • The effect of phospholipids on the activation of protein C by the human thrombin-thrombomodulin complex
    • Freyssinet JM, Gauchy J, Cazenave JP. The effect of phospholipids on the activation of protein C by the human thrombin-thrombomodulin complex. Biochem J 1986;238:151-157.
    • (1986) Biochem J , vol.238 , pp. 151-157
    • Freyssinet, J.M.1    Gauchy, J.2    Cazenave, J.P.3
  • 80
    • 0027997187 scopus 로고
    • Enhancement of thrombin-thrombomodulin-catalysed protein C activation by phosphatidylethanolamine containing unsaturated fatty acids: Possible physiological significance of phosphatidylethanolamine in anticoagulant activity of thrombomodulin
    • Horie S, Ishii H, Hara H, Kazama M. Enhancement of thrombin-thrombomodulin-catalysed protein C activation by phosphatidylethanolamine containing unsaturated fatty acids: possible physiological significance of phosphatidylethanolamine in anticoagulant activity of thrombomodulin. Biochem J 1994;301:683-691.
    • (1994) Biochem J , vol.301 , pp. 683-691
    • Horie, S.1    Ishii, H.2    Hara, H.3    Kazama, M.4
  • 81
    • 0024320616 scopus 로고
    • The active site of the thrombin-thrombomodulin complex. A fluorescence energy transfer measurement of its distance above the membrane surface
    • Lu RL, Esmon NL, Esmon CT, Johnson AE. The active site of the thrombin-thrombomodulin complex. A fluorescence energy transfer measurement of its distance above the membrane surface. J Biol Chem 1989;264:12956-12962.
    • (1989) J Biol Chem , vol.264 , pp. 12956-12962
    • Lu, R.L.1    Esmon, N.L.2    Esmon, C.T.3    Johnson, A.E.4
  • 82
    • 0029840317 scopus 로고    scopus 로고
    • The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study
    • Sunnerhagen M, Olah GA, Stenflo J, Forsen S, Drakenberg T, Trewhella J. The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study. Biochemistry 1996;35:11547-11559.
    • (1996) Biochemistry , vol.35 , pp. 11547-11559
    • Sunnerhagen, M.1    Olah, G.A.2    Stenflo, J.3    Forsen, S.4    Drakenberg, T.5    Trewhella, J.6
  • 83
    • 0032578548 scopus 로고    scopus 로고
    • Effect of high and low molecular weight heparins on thrombin-thrombomodulin interaction and protein C activation
    • De Cristofaro R, De Candia E, Landolfi R. Effect of high and low molecular weight heparins on thrombin-thrombomodulin interaction and protein C activation. Circulation 1998;98:1297-1301.
    • (1998) Circulation , vol.98 , pp. 1297-1301
    • De Cristofaro, R.1    De Candia, E.2    Landolfi, R.3
  • 84
    • 0031755765 scopus 로고    scopus 로고
    • Structure-function relationships in serpins: Current concepts and controversies
    • Gils A, Declerck PJ. Structure-function relationships in serpins: current concepts and controversies. Thromb Haemost 1998;80:531-541.
    • (1998) Thromb Haemost , vol.80 , pp. 531-541
    • Gils, A.1    Declerck, P.J.2
  • 85
    • 0025831251 scopus 로고
    • Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects
    • Olson ST, Bjork I. Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects. J Biol Chem 1991;266:6353-6364.
    • (1991) J Biol Chem , vol.266 , pp. 6353-6364
    • Olson, S.T.1    Bjork, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.