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Volumn 122, Issue 16, 2013, Pages 2777-2783

Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilis

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 5A; MEIZOTHROMBIN; PROTHROMBIN; PROTHROMBINASE COMPLEX; SNAKE VENOM; THROMBIN; UNCLASSIFIED DRUG;

EID: 84887052679     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2013-06-511733     Document Type: Article
Times cited : (64)

References (48)
  • 1
    • 70350512348 scopus 로고    scopus 로고
    • Coagulation and innate immune responses: Can we view them separately?
    • Delvaeye M, Conway EM. Coagulation and innate immune responses: can we view them separately? Blood. 2009;114(12):2367-2374.
    • (2009) Blood , vol.114 , Issue.12 , pp. 2367-2374
    • Delvaeye, M.1    Conway, E.M.2
  • 2
    • 84871505285 scopus 로고    scopus 로고
    • Thrombosis as an intravascular effector of innate immunity
    • Engelmann B, Massberg S. Thrombosis as an intravascular effector of innate immunity. Nat Rev Immunol. 2013;13(1):34-45.
    • (2013) Nat Rev Immunol. , vol.13 , Issue.1 , pp. 34-45
    • Engelmann, B.1    Massberg, S.2
  • 3
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood clotting
    • Davie EW, Ratnoff OD. Waterfall sequence for intrinsic blood clotting. Science. 1964;145(3638):1310-1312.
    • (1964) Science , vol.145 , Issue.3638 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 4
    • 37049044629 scopus 로고
    • An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier
    • MacFarlane RG. An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier. Nature. 1964;202:498-499.
    • (1964) Nature , vol.202 , pp. 498-499
    • MacFarlane, R.G.1
  • 7
    • 0025217011 scopus 로고
    • Prothrombinase complex assembly. Contributions of protein-protein and protein-membrane interactions toward complex formation
    • Krishnaswamy S. Prothrombinase complex assembly. Contributions of protein-protein and protein-membrane interactions toward complex formation. J Biol Chem. 1990;265(7):3708-3718.
    • (1990) J Biol Chem. , vol.265 , Issue.7 , pp. 3708-3718
    • Krishnaswamy, S.1
  • 8
    • 0022975591 scopus 로고
    • The prothrombinase-catalyzed activation of prothrombin proceeds through the intermediate meizothrombin in an ordered, sequential reaction
    • Krishnaswamy S, Mann KG, Nesheim ME. The prothrombinase-catalyzed activation of prothrombin proceeds through the intermediate meizothrombin in an ordered, sequential reaction. J Biol Chem. 1986;261(19):8977-8984.
    • (1986) J Biol Chem. , vol.261 , Issue.19 , pp. 8977-8984
    • Krishnaswamy, S.1    Mann, K.G.2    Nesheim, M.E.3
  • 9
    • 36349026346 scopus 로고    scopus 로고
    • Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase
    • Hacisalihoglu A, Panizzi P, Bock PE, Camire RM, Krishnaswamy S. Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase. J Biol Chem. 2007;282(45):32974- 32982.
    • (2007) J Biol Chem. , vol.282 , Issue.45 , pp. 32974-32982
    • Hacisalihoglu, A.1    Panizzi, P.2    Bock, P.E.3    Camire, R.M.4    Krishnaswamy, S.5
  • 10
    • 33646780547 scopus 로고    scopus 로고
    • Molecular evolution caught in action: Gene duplication and evolution of molecular isoforms of prothrombin activators in Pseudonaja textilis (brown snake)
    • Reza MA, Minh Le TN, Swarup S, Manjunatha Kini R. Molecular evolution caught in action: gene duplication and evolution of molecular isoforms of prothrombin activators in Pseudonaja textilis (brown snake). J Thromb Haemost. 2006;4(6):1346-1353.
    • (2006) J Thromb Haemost. , vol.4 , Issue.6 , pp. 1346-1353
    • Reza, M.A.1    Minh Le, T.N.2    Swarup, S.3    Manjunatha Kini, R.4
  • 11
    • 70149107327 scopus 로고    scopus 로고
    • Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations
    • Bos MH, Boltz M, St Pierre L, et al. Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations. Blood. 2009;114(3):686-692.
    • (2009) Blood , vol.114 , Issue.3 , pp. 686-692
    • Bos, M.H.1    Boltz, M.2    St Pierre, L.3
  • 12
    • 77956279561 scopus 로고    scopus 로고
    • NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation
    • Lechtenberg BC, Johnson DJ, Freund SM, Huntington JA. NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation. Proc Natl Acad Sci USA. 2010;107(32):14087-14092.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.32 , pp. 14087-14092
    • Lechtenberg, B.C.1    Johnson, D.J.2    Freund, S.M.3    Huntington, J.A.4
  • 15
    • 0032538320 scopus 로고    scopus 로고
    • Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa
    • Wei A, Alexander RS, Duke J, Ross H, Rosenfeld SA, Chang CH. Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J Mol Biol. 1998;283(1):147-154.
    • (1998) J Mol Biol. , vol.283 , Issue.1 , pp. 147-154
    • Wei, A.1    Alexander, R.S.2    Duke, J.3    Ross, H.4    Rosenfeld, S.A.5    Chang, C.H.6
  • 16
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr. 1997;53(Pt 3):240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr. , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 18
    • 0034567210 scopus 로고    scopus 로고
    • Comparative protein structure modeling. Introduction and practical examples with modeller
    • Sánchez R, Sali A. Comparative protein structure modeling. Introduction and practical examples with modeller. Methods Mol Biol. 2000;143:97-129.
    • (2000) Methods Mol Biol. , vol.143 , pp. 97-129
    • Sánchez, R.1    Sali, A.2
  • 19
    • 0027304964 scopus 로고
    • Structure of human des (1-45) factor Xa at 2.2 A resolution
    • Padmanabhan K, Padmanabhan KP, Tulinsky A, et al. Structure of human des (1-45) factor Xa at 2.2 A resolution. J Mol Biol. 1993;232(3):947-966.
    • (1993) J Mol Biol. , vol.232 , Issue.3 , pp. 947-966
    • Padmanabhan, K.1    Padmanabhan, K.P.2    Tulinsky, A.3
  • 21
    • 84864386285 scopus 로고    scopus 로고
    • A bipartite autoinhibitory region within the B-domain suppresses function in factor V
    • Bos MH, Camire RM. A bipartite autoinhibitory region within the B-domain suppresses function in factor V. J Biol Chem. 2012;287(31):26342-26351.
    • (2012) J Biol Chem. , vol.287 , Issue.31 , pp. 26342-26351
    • Bos, M.H.1    Camire, R.M.2
  • 22
    • 0017348682 scopus 로고
    • Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin
    • Fehlhammer H, Bode W, Huber R. Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin. J Mol Biol. 1977;111(4):415-438.
    • (1977) J Mol Biol. , vol.111 , Issue.4 , pp. 415-438
    • Fehlhammer, H.1    Bode, W.2    Huber, R.3
  • 23
    • 51049092534 scopus 로고    scopus 로고
    • Mapping of the factor Xa binding site on factor Va by site-directed mutagenesis
    • Steen M, Tran S, Autin L, Villoutreix BO, Tholander AL, Dahlbäck B. Mapping of the factor Xa binding site on factor Va by site-directed mutagenesis. J Biol Chem. 2008;283(30):20805-20812.
    • (2008) J Biol Chem. , vol.283 , Issue.30 , pp. 20805-20812
    • Steen, M.1    Tran, S.2    Autin, L.3    Villoutreix, B.O.4    Tholander, A.L.5    Dahlbäck, B.6
  • 24
    • 0030843304 scopus 로고    scopus 로고
    • Activated protein C cleavage of factor Va leads to dissociation of the A2 domain
    • Mann KG, Hockin MF, Begin KJ, Kalafatis M. Activated protein C cleavage of factor Va leads to dissociation of the A2 domain. J Biol Chem. 1997;272(33):20678-20683.
    • (1997) J Biol Chem. , vol.272 , Issue.33 , pp. 20678-20683
    • Mann, K.G.1    Hockin, M.F.2    Begin, K.J.3    Kalafatis, M.4
  • 25
    • 0021718109 scopus 로고
    • Loss of prothrombin and of factor Xa-factor Va interactions upon inactivation of factor Va by activated protein C
    • Guinto ER, Esmon CT. Loss of prothrombin and of factor Xa-factor Va interactions upon inactivation of factor Va by activated protein C. J Biol Chem. 1984;259(22):13986-13992.
    • (1984) J Biol Chem. , vol.259 , Issue.22 , pp. 13986-13992
    • Guinto, E.R.1    Esmon, C.T.2
  • 26
    • 0347997285 scopus 로고    scopus 로고
    • Defining the factor Xa-binding site on factor Va by site-directed glycosylation
    • Steen M, Villoutreix BO, Norstrøm EA, Yamazaki T, Dahlbäck B. Defining the factor Xa-binding site on factor Va by site-directed glycosylation. J Biol Chem. 2002;277(51):50022-50029.
    • (2002) J Biol Chem. , vol.277 , Issue.51 , pp. 50022-50029
    • Steen, M.1    Villoutreix, B.O.2    Norstrøm, E.A.3    Yamazaki, T.4    Dahlbäck, B.5
  • 27
    • 0028148074 scopus 로고
    • Functional properties of human factor Va lacking the Asp683-Arg709 domain of the heavy chain
    • Bakker HM, Tans G, Thomassen MC, et al. Functional properties of human factor Va lacking the Asp683-Arg709 domain of the heavy chain. J Biol Chem. 1994;269(32):20662-20667.
    • (1994) J Biol Chem. , vol.269 , Issue.32 , pp. 20662-20667
    • Bakker, H.M.1    Tans, G.2    Thomassen, M.C.3
  • 28
    • 33646831644 scopus 로고    scopus 로고
    • Role of Hirudin-like factor Va heavy chain sequences in prothrombinase function
    • Toso R, Camire RM. Role of Hirudin-like factor Va heavy chain sequences in prothrombinase function. J Biol Chem. 2006;281(13):8773-8779.
    • (2006) J Biol Chem. , vol.281 , Issue.13 , pp. 8773-8779
    • Toso, R.1    Camire, R.M.2
  • 29
    • 42449150052 scopus 로고    scopus 로고
    • Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex
    • Li W, Adams TE, Nangalia J, Esmon CT, Huntington JA. Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex. Proc Natl Acad Sci USA. 2008;105(12):4661-4666.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.12 , pp. 4661-4666
    • Li, W.1    Adams, T.E.2    Nangalia, J.3    Esmon, C.T.4    Huntington, J.A.5
  • 30
    • 0034602993 scopus 로고    scopus 로고
    • Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding
    • Rezaie AR. Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding. J Biol Chem. 2000;275(5):3320-3327.
    • (2000) J Biol Chem. , vol.275 , Issue.5 , pp. 3320-3327
    • Rezaie, A.R.1
  • 31
    • 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(21):9796-9800.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.21 , pp. 9796-9800
    • Brandstetter, H.1    Bauer, M.2    Huber, R.3    Lollar, P.4    Bode, W.5
  • 32
    • 0023518606 scopus 로고
    • The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex
    • Husten EJ, Esmon CT, Johnson AE. The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex. J Biol Chem. 1987;262(27):12953-12961.
    • (1987) J Biol Chem. , vol.262 , Issue.27 , pp. 12953-12961
    • Husten, E.J.1    Esmon, C.T.2    Johnson, A.E.3
  • 33
    • 0022552672 scopus 로고
    • A domain of membrane-bound blood coagulation factor Va is located far from the phospholipid surface. A fluorescence energy transfer measurement
    • Isaacs BS, Husten EJ, Esmon CT, Johnson AE. A domain of membrane-bound blood coagulation factor Va is located far from the phospholipid surface. A fluorescence energy transfer measurement. Biochemistry. 1986;25(17):4958-4969.
    • (1986) Biochemistry , vol.25 , Issue.17 , pp. 4958-4969
    • Isaacs, B.S.1    Husten, E.J.2    Esmon, C.T.3    Johnson, A.E.4
  • 34
    • 84881227791 scopus 로고    scopus 로고
    • Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation [published online ahead of print June 17, 2013]
    • Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation [published online ahead of print June 17, 2013]. J Biol Chem.
    • J Biol Chem.
    • Pozzi, N.1    Chen, Z.2    Gohara, D.W.3    Niu, W.4    Heyduk, T.5    Di Cera, E.6
  • 35
    • 0026610682 scopus 로고
    • The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1
    • Soriano-Garcia M, Padmanabhan K, de Vos AM, Tulinsky A. The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1. Biochemistry. 1992;31(9):2554-2566.
    • (1992) Biochemistry , vol.31 , Issue.9 , pp. 2554-2566
    • Soriano-Garcia, M.1    Padmanabhan, K.2    De Vos, A.M.3    Tulinsky, A.4
  • 36
    • 78650623661 scopus 로고    scopus 로고
    • Crystal structure of prethrombin-1
    • Chen Z, Pelc LA, Di Cera E. Crystal structure of prethrombin-1. Proc Natl Acad Sci USA. 2010;107(45):19278-19283.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.45 , pp. 19278-19283
    • Chen, Z.1    Pelc, L.A.2    Di Cera, E.3
  • 37
    • 84865304308 scopus 로고    scopus 로고
    • A molecular model of the human prothrombinase complex
    • Tanaka K, Davie E, Ikeda Y, Iwanaga S, Saito H, Sueishi K, eds, Kyoto, Japan: Springer
    • Everse S, Adams T, Mann K. A molecular model of the human prothrombinase complex. In: Tanaka K, Davie E, Ikeda Y, Iwanaga S, Saito H, Sueishi K, eds. Recent Advances in Thrombosis and Hemostasis 2008. Kyoto, Japan: Springer; 2008:107-132
    • (2008) Recent Advances in Thrombosis and Hemostasis 2008 , pp. 107-132
    • Everse, S.1    Adams, T.2    Mann, K.3
  • 38
    • 0034528766 scopus 로고    scopus 로고
    • The Gla domain of human prothrombin has a binding site for factor Va
    • Blostein MD, Rigby AC, Jacobs M, Furie B, Furie BC. The Gla domain of human prothrombin has a binding site for factor Va. J Biol Chem. 2000;275(48):38120-38126.
    • (2000) J Biol Chem. , vol.275 , Issue.48 , pp. 38120-38126
    • Blostein, M.D.1    Rigby, A.C.2    Jacobs, M.3    Furie, B.4    Furie, B.C.5
  • 39
    • 11144229671 scopus 로고    scopus 로고
    • Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin
    • Orcutt SJ, Krishnaswamy S. Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin. J Biol Chem. 2004;279(52):54927-54936.
    • (2004) J Biol Chem. , vol.279 , Issue.52 , pp. 54927-54936
    • Orcutt, S.J.1    Krishnaswamy, S.2
  • 40
    • 22544469092 scopus 로고    scopus 로고
    • Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase
    • Bianchini EP, Orcutt SJ, Panizzi P, Bock PE, Krishnaswamy S. Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase. Proc Natl Acad Sci USA. 2005;102(29):10099-10104.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.29 , pp. 10099-10104
    • Bianchini, E.P.1    Orcutt, S.J.2    Panizzi, P.3    Bock, P.E.4    Krishnaswamy, S.5
  • 41
    • 0037470249 scopus 로고    scopus 로고
    • Analysis of the kinetics of prothrombin activation and evidence that two equilibrating forms of prothrombinase are involved in the process
    • Brufatto N, Nesheim ME. Analysis of the kinetics of prothrombin activation and evidence that two equilibrating forms of prothrombinase are involved in the process. J Biol Chem. 2003;278(9):6755-6764.
    • (2003) J Biol Chem. , vol.278 , Issue.9 , pp. 6755-6764
    • Brufatto, N.1    Nesheim, M.E.2
  • 42
    • 84865763235 scopus 로고    scopus 로고
    • Meizothrombin is an unexpectedly zymogen-like variant of thrombin
    • Bradford HN, Krishnaswamy S. Meizothrombin is an unexpectedly zymogen-like variant of thrombin. J Biol Chem. 2012;287(36):30414-30425.
    • (2012) J Biol Chem. , vol.287 , Issue.36 , pp. 30414-30425
    • Bradford, H.N.1    Krishnaswamy, S.2
  • 44
    • 33646581724 scopus 로고    scopus 로고
    • Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation
    • Johnson DJ, Li W, Adams TE, Huntington JA. Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation. EMBO J. 2006;25(9):2029-2037.
    • (2006) EMBO J. , vol.25 , Issue.9 , pp. 2029-2037
    • Johnson, D.J.1    Li, W.2    Adams, T.E.3    Huntington, J.A.4
  • 45
    • 79959569996 scopus 로고    scopus 로고
    • Allosteric activation of coagulation factor VIIa
    • Persson E, Olsen OH. Allosteric activation of coagulation factor VIIa. Front Biosci. 2011;16:3156-3163.
    • (2011) Front Biosci. , vol.16 , pp. 3156-3163
    • Persson, E.1    Olsen, O.H.2
  • 46
    • 12644264319 scopus 로고    scopus 로고
    • Protein engineering thrombin for optimal specificity and potency of anticoagulant activity in vivo
    • Tsiang M, Paborsky LR, Li WX, et al. Protein engineering thrombin for optimal specificity and potency of anticoagulant activity in vivo. Biochemistry. 1996;35(51):16449-16457.
    • (1996) Biochemistry , vol.35 , Issue.51 , pp. 16449-16457
    • Tsiang, M.1    Paborsky, L.R.2    Li, W.X.3
  • 47
    • 78650988916 scopus 로고    scopus 로고
    • Zymogen-like factor Xa variants restore thrombin generation and effectively bypass the intrinsic pathway in vitro
    • Bunce MW, Toso R, Camire RM. Zymogen-like factor Xa variants restore thrombin generation and effectively bypass the intrinsic pathway in vitro. Blood. 2011;117(1):290-298.
    • (2011) Blood , vol.117 , Issue.1 , pp. 290-298
    • Bunce, M.W.1    Toso, R.2    Camire, R.M.3
  • 48
    • 84868583648 scopus 로고    scopus 로고
    • Stable complex formation between serine protease inhibitor and zymogen: Coagulation factor X cleaves the Arg393-Ser394 bond in a reactive centre loop of antithrombin in the presence of heparin
    • Nakatomi Y, Tsuji M, Gokudan S, et al. Stable complex formation between serine protease inhibitor and zymogen: coagulation factor X cleaves the Arg393-Ser394 bond in a reactive centre loop of antithrombin in the presence of heparin. J Biochem. 2012;152(5):463-470.
    • (2012) J Biochem. , vol.152 , Issue.5 , pp. 463-470
    • Nakatomi, Y.1    Tsuji, M.2    Gokudan, S.3


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