메뉴 건너뛰기




Volumn 276, Issue 11, 2009, Pages 3099-3109

Activation loop 3 and the 170 loop interact in the active conformation of coagulation factor VIIa

Author keywords

Activation loop; Allosteric activation; Factor VIIa; Initiation of coagulation; Tissue factor

Indexed keywords

ARGININE; BLOOD CLOTTING FACTOR 7A; G372A FVIIA ENZYME; GLYCINE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 65549161856     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07028.x     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 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
  • 2
    • 0028109290 scopus 로고
    • Membrane-dependent reactions in blood coagulation: Role of the vitamin K-dependent enzyme complexes
    • DOI 10.1016/0925-4439(94)90086-8
    • Kalafatis M, Swords NA, Rand MD Mann KG (1994) Membrane-dependent reactions in blood coagulation: role of the vitamin K-dependent enzyme complexes. Biochim Biophys Acta 1227, 113 129. (Pubitemid 24371738)
    • (1994) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1227 , Issue.3 , pp. 113-129
    • Kalafatis, M.1    Swords, N.A.2    Mann, K.G.3
  • 3
    • 0029903723 scopus 로고    scopus 로고
    • The location of the active site of blood coagulation factor VIIa above the membrane surface and its reorientation upon association with tissue factor: A fluorescence energy transfer study
    • DOI 10.1074/jbc.271.45.28168
    • McCallum CD, Hapak RC, Neuenschwander PF, Morrissey JH Johnson AE (1996) The location of the active site of blood coagulation factor VIIa above the membrane surface and its reorientation upon association with tissue factor. A fluorescence energy transfer study. J Biol Chem 271, 28168 28175. (Pubitemid 26374626)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.45 , pp. 28168-28175
    • McCallum, C.D.1    Hapak, R.C.2    Neuenschwander, P.F.3    Morrissey, J.H.4    Johnson, A.E.5
  • 4
    • 0031649079 scopus 로고    scopus 로고
    • Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa
    • DOI 10.1016/S1050-1738(98)00031-0, PII S1050173898000310
    • Ruf W Dickinson CD (1998) Allosteric regulation of the cofactor-dependent serine protease coagulation factor VIIa. Trends Cardiovasc Med 8, 350 356. (Pubitemid 28565199)
    • (1998) Trends in Cardiovascular Medicine , vol.8 , Issue.8 , pp. 350-356
    • Ruf, W.1    Dickinson, C.D.2
  • 6
    • 0033579442 scopus 로고    scopus 로고
    • Electron crystallography of human blood coagulation factor VIII bound to phospholipid monolayers
    • DOI 10.1074/jbc.274.51.36573
    • Kemball-Cook G, Johnson DJD, Tuddenham EGD Harlos K (1999) Crystal structure of active site-inhibited human coagulation factor VIIa (des-Gla). J Struct Biol 127, 213 223. (Pubitemid 30005268)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.51 , pp. 36573-36578
    • Stoylova, S.S.1    Lenting, P.J.2    Kemball-Cook, G.3    Holzenburg, A.4
  • 9
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • DOI 10.1038/380041a0
    • Banner DW, D'Arcy A, Chène C, Winkler FK, Guha A, Konigsberg WH, Nemerson Y Kirchhofer D (1996) The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature 380, 41 46. (Pubitemid 26076234)
    • (1996) Nature , vol.380 , Issue.6569 , pp. 41-46
    • Banner, D.W.1    D'Arcy, A.2    Chene, C.3    Winkler, F.K.4    Guha, A.5    Konigsberg, W.H.6    Nemerson, Y.7    Kirchhofer, D.8
  • 10
    • 0033524955 scopus 로고    scopus 로고
    • Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant
    • DOI 10.1006/jmbi.1998.2452
    • Zhang E, St Charles R Tulinsky A (1999) Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant. J Mol Biol 285, 2089 2104. (Pubitemid 29078173)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 2089-2104
    • Zhang, E.1    St. Charles, R.2    Tulinsky, A.3
  • 11
    • 33747702876 scopus 로고    scopus 로고
    • High resolution structures of p-aminobenzamidine- and benzamidine-VIIa/soluble tissue factor
    • Bajaj SP, Schmidt AE, Agah S, Bajaj MS Padmanabhan K (2006) High resolution structures of p-aminobenzamidine- and benzamidine-VIIa/soluble tissue factor. J Biol Chem 281, 24873 24888.
    • (2006) J Biol Chem , vol.281 , pp. 24873-24888
    • Bajaj, S.P.1    Schmidt, A.E.2    Agah, S.3    Bajaj, M.S.4    Padmanabhan, K.5
  • 12
    • 0035916953 scopus 로고    scopus 로고
    • Substitution of aspartic acid for methionine-306 in factor VIIa abolishes the allosteric linkage between the active site and the binding interface with tissue factor
    • DOI 10.1021/bi001612z
    • Persson E, Nielsen LS Olsen OH (2001) Substitution of aspartic acid for methionine-306 in factor VIIa abolishes the allosteric linkage between the active site and the binding interface with tissue factor. Biochemistry 40, 3251 3256. (Pubitemid 32221625)
    • (2001) Biochemistry , vol.40 , Issue.11 , pp. 3251-3256
    • Persson, E.1    Nielsen, L.S.2    Olsen, O.H.3
  • 14
    • 0035794140 scopus 로고    scopus 로고
    • 156 Contributes to the Labile Enzyme Conformation of Coagulation Factor VIIa
    • DOI 10.1074/jbc.M004726200
    • 156 contributes to the labile enzyme conformation of coagulation factor VIIa. J Biol Chem 276, 6616 6620. (Pubitemid 37373526)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.9 , pp. 6616-6620
    • Petrovan, R.J.1    Ruf, W.2
  • 16
    • 0037199426 scopus 로고    scopus 로고
    • Role of zymogenicity-determining residues of coagulation factor VII/VIIa in cofactor interaction and macromolecular substrate recognition
    • Petrovan RJ Ruf W (2002) Role of zymogenicity-determining residues of coagulation factor VII/VIIa in cofactor interaction and macromolecular substrate recognition. Biochemistry 41, 9302 9309.
    • (2002) Biochemistry , vol.41 , pp. 9302-9309
    • Petrovan, R.J.1    Ruf, W.2
  • 17
    • 0036444244 scopus 로고    scopus 로고
    • Assignment of molecular properties of a superactive coagulation factor VIIa variant to individual amino acid changes
    • DOI 10.1046/j.1432-1033.2002.03323.x
    • Persson E Olsen OH (2002) Assignment of molecular properties of a superactive coagulation factor VIIa variant to individual amino acid changes. Eur J Biochem 269, 5950 5955. (Pubitemid 35425592)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.23 , pp. 5950-5955
    • Persson, E.1    Olsen, O.H.2
  • 18
    • 0028225878 scopus 로고
    • Identification of regions of bovine factor VII essential for binding to tissue factor
    • Higashi S, Nishimura H, Aita K Iwanaga S (1994) Identification of regions of bovine factor VII essential for binding to tissue factor. J Biol Chem 269, 18891 18898. (Pubitemid 24226203)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.29 , pp. 18891-18898
    • Higashi, S.1    Nishimura, H.2    Aita, K.3    Iwanaga, S.4
  • 19
    • 0035800804 scopus 로고    scopus 로고
    • Substitution of Valine for Leucine 305 in Factor VIIa Increases the Intrinsic Enzymatic Activity
    • DOI 10.1074/jbc.M102187200
    • Persson E, Bak H Olsen OH (2001) Substitution of valine for leucine 305 in factor VIIa increases the intrinsic enzymatic activity. J Biol Chem 276, 29195 29199. (Pubitemid 37452009)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.31 , pp. 29195-29199
    • Persson, E.1    Bak, H.2    Olsen, O.H.3
  • 20
    • 2342503204 scopus 로고    scopus 로고
    • Augmented intrinsic activity of Factor VIIa by replacement of residues 305, 314, 337 and 374: Evidence of two unique mutational mechanisms of activity enhancement
    • DOI 10.1042/BJ20031596
    • Persson E, Bak H, Østergaard A Olsen OH (2004) Augmented intrinsic activity of factor VIIa by replacement of residues 305, 314, 337 and 374: evidence of two unique mutational mechanisms of activity enhancement. Biochem J 379, 497 503. (Pubitemid 38570123)
    • (2004) Biochemical Journal , vol.379 , Issue.2 , pp. 497-503
    • Persson, E.1    Bak, H.2    Ostergaard, A.3    Olsen, O.H.4
  • 21
    • 0034941729 scopus 로고    scopus 로고
    • The factor VII zymogen structure reveals reregistration of Beta strands during activation
    • DOI 10.1016/S0969-2126(01)00624-4, PII S0969212601006244
    • Eigenbrot C, Kirchhofer D, Dennis MS, Santell L, Lazarus RA, Stamos J Ultsch MH (2001) The factor VII zymogen structure reveals reregistration of strands during activation. Structure 9, 627 636. (Pubitemid 32695587)
    • (2001) Structure , vol.9 , Issue.7 , pp. 627-636
    • Eigenbrot, C.1    Kirchhofer, D.2    Dennis, M.S.3    Santell, L.4    Lazarus, R.A.5    Stamos, J.6    Ultsch, M.H.7
  • 22
    • 25144522771 scopus 로고    scopus 로고
    • A reconsideration of the evidence for structural reorganization in FVII zymogen [8]
    • DOI 10.1111/j.1538-7836.2005.01433.x
    • Perera L Pedersen LG (2005) A reconsideration of the evidence for structural reorganization in FVII zymogen. J Thromb Haemost 3, 1543 1545. (Pubitemid 41725220)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.7 , pp. 1543-1545
    • Perera, L.1    Pedersen, L.G.2
  • 23
    • 17744362278 scopus 로고    scopus 로고
    • Disulfide locked variants of factor VIIa with a restricted Beta-strand conformation have enhanced enzymatic activity
    • DOI 10.1110/ps.041097505
    • Maun HR, Eigenbrot C, Raab H, Arnott D, Phu L, Bullens S Lazarus RA (2005) Disulfide locked variants of factor VIIa with a restricted -strand conformation have enhanced enzymatic activity. Protein Sci 14, 1171 1180. (Pubitemid 40577797)
    • (2005) Protein Science , vol.14 , Issue.5 , pp. 1171-1180
    • Maun, H.R.1    Eigenbrot, C.2    Raab, H.3    Arnott, D.4    Phu, L.5    Bullens, S.6    Lazarus, R.A.7
  • 24
    • 8344226974 scopus 로고    scopus 로고
    • Prevention of Beta strand movement into a zymogen-like position does not confer higher activity to coagulation factor VIIa
    • DOI 10.1021/bi048721o
    • Olsen OH, Nielsen PF Persson E (2004) Prevention of strand movement into a zymogen-like position does not confer higher activity to coagulation factor VIIa. Biochemistry 43, 14096 14103. (Pubitemid 39482759)
    • (2004) Biochemistry , vol.43 , Issue.44 , pp. 14096-14103
    • Olsen, O.H.1    Nielsen, P.F.2    Persson, E.3
  • 26
    • 33947720248 scopus 로고    scopus 로고
    • A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation
    • DOI 10.1110/ps.062504907
    • Olsen OH, Rand KD, Østergaard H Persson E (2007) A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation. Protein Sci 16, 671 682. (Pubitemid 46506996)
    • (2007) Protein Science , vol.16 , Issue.4 , pp. 671-682
    • Olsen, O.H.1    Rand, K.D.2    Ostergaard, H.3    Persson, E.4
  • 28
    • 0017348682 scopus 로고
    • Crystal structure of bovine trypsinogen at 1.8A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin
    • Fehlhammer H, Bode W Huber R (1977) Crystal structure of bovine trypsinogen at 1.8 a resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin. J Mol Biol 111, 415 438. (Pubitemid 8090356)
    • (1977) Journal of Molecular Biology , vol.111 , Issue.4 , pp. 415-438
    • Fehlhammer, H.1    Bode, W.2    Huber, R.3
  • 29
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R Bode W (1978) Structural basis of the activation and action of trypsin. Acc Chem Res 11, 114 122.
    • (1978) Acc Chem Res , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 30
    • 0035907354 scopus 로고    scopus 로고
    • Factor VIIa Modified in the 170 Loop Shows Enhanced Catalytic Activity but Does Not Change the Zymogen-like Property
    • DOI 10.1074/jbc.M009206200
    • Soejima K, Mizuguchi J, Yuguchi M, Nakagaki T, Higashi S Iwanaga S (2001) Factor VIIa modified in the 170 loop shows enhanced catalytic activity but does not change the zymogen-like property. J Biol Chem 276, 17229 17235. (Pubitemid 37411529)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.20 , pp. 17229-17235
    • Soejima, K.1    Mizuguchi, J.2    Yuguchi, M.3    Nakagaki, T.4    Higashi, S.5    Iwanaga, S.6
  • 31
    • 0033588095 scopus 로고    scopus 로고
    • Macromolecular substrate affinity for the tissue factor-factor VIIa complex is independent of scissile bond docking
    • Shobe J, Dickinson CD, Edgington TS Ruf W (1999) Macromolecular substrate affinity for the tissue factor-factor VIIa complex is independent of scissile bond docking. J Biol Chem 274, 24171 24175. (Pubitemid 129528464)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.34 , pp. 24171-24175
    • Shobe, J.1    Dickinson, C.D.2    Edgington, T.S.3    Ruf, W.4
  • 32
    • 0034665994 scopus 로고    scopus 로고
    • Exosite interactions determine the affinity of factor X for the extrinsic Xase complex
    • Baugh RJ, Dickinson CD, Ruf W Krishnaswamy S (2000) Exosite interactions determine the affinity of factor X for the extrinsic Xase complex. J Biol Chem 275, 28826 28833.
    • (2000) J Biol Chem , vol.275 , pp. 28826-28833
    • Baugh, R.J.1    Dickinson, C.D.2    Ruf, W.3    Krishnaswamy, S.4
  • 33
    • 17644371341 scopus 로고    scopus 로고
    • Exosite-driven substrate specificity and function in coagulation
    • DOI 10.1111/j.1538-7836.2004.01021.x
    • Krishnaswamy S (2005) Exosite-driven substrate specificity and function in coagulation. J Thromb Haemost 3, 54 67. (Pubitemid 41647115)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.1 , pp. 54-67
    • Krishnaswamy, S.1
  • 36
    • 0023784390 scopus 로고
    • Amino acid sequence and posttranslational modifications of human factor VII(a) from plasma and transfected baby hamster kidney cells
    • DOI 10.1021/bi00420a030
    • Thim L, Bjoern S, Christensen M, Nicolaisen EM, Lund-Hansen T, Pedersen A Hedner U (1988) Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. Biochemistry 27, 7785 7793. (Pubitemid 18247534)
    • (1988) Biochemistry , vol.27 , Issue.20 , pp. 7785-7793
    • Thim, L.1    Bjoern, S.2    Christensen, M.3    Nicolaisen, E.M.4    Lund-Hansen, T.5    Pedersen, A.H.6    Hedner, U.7
  • 37
    • 0030017619 scopus 로고    scopus 로고
    • 2+ and tissue factor studied using circular dichroism spectroscopy
    • 2+and tissue factor studied using circular dichroism spectroscopy. Protein Sci 5, 1531 1540. (Pubitemid 26257218)
    • (1996) Protein Science , vol.5 , Issue.8 , pp. 1531-1540
    • Freskgard, P.-O.1    Olsen, O.H.2    Persson, E.3
  • 38
    • 0029951107 scopus 로고    scopus 로고
    • Site-directed mutagenesis but not-carboxylation of Glu-35 in factor VIIa affects the association with tissue factor
    • DOI 10.1016/0014-5793(96)00400-0, PII S0014579396004000
    • Persson E Nielsen LS (1996) Site-directed mutagenesis but not-carboxylation of Glu-35 in factor VIIa affects the association with tissue factor. FEBS Lett 385, 241 243. (Pubitemid 126334550)
    • (1996) FEBS Letters , vol.385 , Issue.3 , pp. 241-243
    • Persson, E.1    Nielsen, L.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.