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Volumn 585, Issue 19, 2011, Pages 3020-3025

Structural basis of coagulation factor v recognition for cleavage by RVV-V

Author keywords

Blood coagulation; Induced fit; Serine proteinase; Snake venom; Substrate recognition

Indexed keywords

ARGININE; BLOOD CLOTTING FACTOR 5; ISOLEUCINE; PROTEINASE; RUSSELL VIPER VENOM FACTOR V ACTIVATOR; UNCLASSIFIED DRUG;

EID: 80053281852     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.08.022     Document Type: Article
Times cited : (27)

References (35)
  • 1
    • 0036124011 scopus 로고    scopus 로고
    • Factor V and thrombotic disease description of a Janus-faced protein
    • DOI 10.1161/01.ATV.0000012665.51263.B7
    • G.A. Nicolaes, and B. Dahlback Factor V and thrombotic disease: description of a janus-faced protein Arterioscler. Thromb. Vasc. Biol. 22 2002 530 538 (Pubitemid 34408730)
    • (2002) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.22 , Issue.4 , pp. 530-538
    • Nicolaes, G.A.F.1    Dahlback, B.2
  • 2
    • 0037220079 scopus 로고    scopus 로고
    • Factor V: A combination of Dr. Jekyll and Mr. Hyde
    • K.G. Mann, and M. Kalafatis Factor V: a combination of Dr. Jekyll and Mr. Hyde Blood 101 2003 20 30
    • (2003) Blood , vol.101 , pp. 20-30
    • Mann, K.G.1    Kalafatis, M.2
  • 4
    • 0020320628 scopus 로고
    • Thrombin-catalyzed activation of human coagulation factor V
    • K. Suzuki, B. Dahlback, and J. Stenflo Thrombin-catalyzed activation of human coagulation factor V J. Biol. Chem. 257 1982 6556 6564 (Pubitemid 12059950)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.11 , pp. 6556-6564
    • Suzuki, K.1    Dahlback, B.2    Stenflo, J.3
  • 5
    • 0018786088 scopus 로고
    • The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity
    • C.T. Esmon The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity J. Biol. Chem. 254 1979 964 973
    • (1979) J. Biol. Chem. , vol.254 , pp. 964-973
    • Esmon, C.T.1
  • 6
    • 0018622772 scopus 로고
    • The contribution of bovine factor V and factor Va to the activity of prothrombinase
    • M.E. Nesheim, J.B. Taswell, and K.G. Mann The contribution of bovine factor V and factor Va to the activity of prothrombinase J. Biol. Chem. 254 1979 10952 10962 (Pubitemid 10163282)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.21 , pp. 10952-10962
    • Nesheim, M.E.1    Taswell, J.B.2    Mann, K.G.3
  • 9
    • 0037064117 scopus 로고    scopus 로고
    • Thrombin-mediated proteolysis of factor V resulting in gradual B-domain release and exposure of the factor Xa-binding site
    • DOI 10.1074/jbc.M204972200
    • M. Steen, and B. Dahlback Thrombin-mediated proteolysis of factor V resulting in gradual B-domain release and exposure of the factor Xa-binding site J. Biol. Chem. 277 2002 38424 38430 (Pubitemid 35154699)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38424-38430
    • Steen, M.1    Dahlback, B.2
  • 10
    • 2442655492 scopus 로고    scopus 로고
    • Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized
    • DOI 10.1074/jbc.M402107200
    • R. Toso, and R.M. Camire Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized J. Biol. Chem. 279 2004 21643 21650 (Pubitemid 38656576)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 21643-21650
    • Toso, R.1    Camire, R.M.2
  • 11
    • 0018907213 scopus 로고
    • The role of phospholipids and factor Va in the prothrombinase complex
    • J. Rosing, G. Tans, J.W. Govers-Riemslag, R.F. Zwaal, and H.C. Hemker The role of phospholipids and factor Va in the prothrombinase complex J. Biol. Chem. 255 1980 274 283 (Pubitemid 10146055)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.1 , pp. 274-283
    • Rosing, J.1    Tans, G.2    Govers-Riemslag, J.W.P.3
  • 13
    • 19544394247 scopus 로고    scopus 로고
    • Snake venom serine proteinases: Sequence homology vs. substrate specificity, a paradox to be solved
    • DOI 10.1016/j.toxicon.2005.02.020, PII S0041010105000759, Snake Toxins and Hemostasis
    • S.M. Serrano, and R.C. Maroun Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved Toxicon 45 2005 1115 1132 (Pubitemid 40732585)
    • (2005) Toxicon , vol.45 , Issue.8 , pp. 1115-1132
    • Serrano, S.M.T.1    Maroun, R.C.2
  • 14
    • 0014500944 scopus 로고
    • Separation from Russell's viper venom of one fraction reacting with factor X and another reacting with factor v
    • S. Schiffman, I. Theodor, and S.I. Rapaport Separation from Russell's viper venom of one fraction reacting with factor X and another reacting with factor V Biochemistry 8 1969 1397 1405
    • (1969) Biochemistry , vol.8 , pp. 1397-1405
    • Schiffman, S.1    Theodor, I.2    Rapaport, S.I.3
  • 15
    • 0024270675 scopus 로고
    • The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-V(α), -Vβ, and -Vγ and their complete amino acid sequences
    • F. Tokunaga, K. Nagasawa, S. Tamura, T. Miyata, S. Iwanaga, and W. Kisiel The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences J. Biol. Chem. 263 1988 17471 17481 (Pubitemid 19029331)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.33 , pp. 17471-17481
    • Tokunaga, F.1    Nagasawa, F.2    Tamura, S.3    Miyata, T.4    Iwanaga, S.5    Kisiel, W.6
  • 16
    • 33748447516 scopus 로고    scopus 로고
    • Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina
    • DOI 10.1002/prot.21051
    • K. Segers, J. Rosing, and G.A. Nicolaes Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina Proteins 64 2006 968 984 (Pubitemid 44420938)
    • (2006) Proteins: Structure, Function and Genetics , vol.64 , Issue.4 , pp. 968-984
    • Segers, K.1    Rosing, J.2    Nicolaes, G.A.F.3
  • 17
    • 0019862464 scopus 로고
    • Purification and characterization of human coagulation factor V
    • W.H. Kane, and P.W. Majerus Purification and characterization of human coagulation factor V J. Biol. Chem. 256 1981 1002 1007 (Pubitemid 11103058)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.2 , pp. 1002-1007
    • Kane, W.H.1    Majerus, P.W.2
  • 18
    • 0015831665 scopus 로고
    • The factor v activating enzyme of Russell's viper venom
    • C.T. Esmon, and C.M. Jackson The factor V activating enzyme of Russell's viper venom Thromb. Res. 2 1973 509 524
    • (1973) Thromb. Res. , vol.2 , pp. 509-524
    • Esmon, C.T.1    Jackson, C.M.2
  • 19
    • 19544362198 scopus 로고    scopus 로고
    • Practical applications of snake venom toxins in haemostasis
    • DOI 10.1016/j.toxicon.2005.02.016, PII S0041010105000796, Snake Toxins and Hemostasis
    • N. Marsh, and V. Williams Practical applications of snake venom toxins in haemostasis Toxicon 45 2005 1171 1181 (Pubitemid 40732589)
    • (2005) Toxicon , vol.45 , Issue.8 , pp. 1171-1181
    • Marsh, N.1    Williams, V.2
  • 20
    • 79960622739 scopus 로고    scopus 로고
    • Diagnostic use of snake venom components in the coagulation laboratory
    • R. Kini, K.J. Clemetson, F.S. Markland, M.A. McLane, T. Morita, Springer Science + Business Media
    • A.M. Perchuc, and M. Wilmer Diagnostic use of snake venom components in the coagulation laboratory R. Kini, K.J. Clemetson, F.S. Markland, M.A. McLane, T. Morita, Toxins and Hemostasis: From Bench to bedside 2010 Springer Science + Business Media 747 766
    • (2010) Toxins and Hemostasis: From Bench to Bedside , pp. 747-766
    • Perchuc, A.M.1    Wilmer, M.2
  • 21
    • 74549131070 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom
    • D. Nakayama, Y. Ben Ammar, and S. Takeda Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 65 2009 1306 1308
    • (2009) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.65 , pp. 1306-1308
    • Nakayama, D.1    Ben Ammar, Y.2    Takeda, S.3
  • 23
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • A.T. Brunger Crystallography and NMR system: A new software suite for macromolecular structure determination Acta Crystallogr. D: Biol. Crystallogr. 54 Pt 5 1998 905 921
    • (1998) Acta Crystallogr. D: Biol. Crystallogr. , vol.54 , Issue.PART 5 , pp. 905-921
    • Brunger, A.T.1
  • 25
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 27
    • 0026657151 scopus 로고
    • The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution
    • P.D. Martin, W. Robertson, D. Turk, R. Huber, W. Bode, and B.F. Edwards The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution J. Biol. Chem. 267 1992 7911 7920
    • (1992) J. Biol. Chem. , vol.267 , pp. 7911-7920
    • Martin, P.D.1    Robertson, W.2    Turk, D.3    Huber, R.4    Bode, W.5    Edwards, B.F.6
  • 28
    • 68949090269 scopus 로고    scopus 로고
    • Structural basis for proteolytic specificity of the human apoptosis-inducing granzyme M
    • L. Wu Structural basis for proteolytic specificity of the human apoptosis-inducing granzyme M J. Immunol. 183 2009 421 429
    • (2009) J. Immunol. , vol.183 , pp. 421-429
    • Wu, L.1
  • 29
    • 0344500853 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of a cDNA for factor v activating enzyme
    • E. Siigur, A. Aaspollu, and J. Siigur Molecular cloning and sequence analysis of a cDNA for factor V activating enzyme Biochem. Biophys. Res. Commun. 262 1999 328 332
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 328-332
    • Siigur, E.1    Aaspollu, A.2    Siigur, J.3
  • 30
    • 0024431034 scopus 로고
    • The refined 1.9 A crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • W. Bode, I. Mayr, U. Baumann, R. Huber, S.R. Stone, and J. Hofsteenge The refined 1.9 A 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. 8 1989 3467 3475 (Pubitemid 19273577)
    • (1989) EMBO Journal , vol.8 , Issue.11 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 31
    • 0028899505 scopus 로고
    • A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning
    • Y. Zhang, A. Wisner, Y. Xiong, and C. Bon A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning J. Biol. Chem. 270 1995 10246 10255
    • (1995) J. Biol. Chem. , vol.270 , pp. 10246-10255
    • Zhang, Y.1    Wisner, A.2    Xiong, Y.3    Bon, C.4
  • 32
    • 0017107996 scopus 로고
    • Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin
    • W. Bode, and R. Huber Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin FEBS Lett. 68 1976 231 236
    • (1976) FEBS Lett. , vol.68 , pp. 231-236
    • Bode, W.1    Huber, R.2
  • 33
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution
    • W. Bode, P. Schwager, and R. Huber The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution J. Mol. Biol. 118 1978 99 112 (Pubitemid 8271375)
    • (1978) Journal of Molecular Biology , vol.118 , Issue.1 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 35
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • I.W. Davis MolProbity: all-atom contacts and structure validation for proteins and nucleic acids Nucleic Acids Res. 35 2007 W375 W383
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1


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