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Volumn 98, Issue 3, 1996, Pages 351-370

Molecular reconstruction and homology modelling of the catalytic domain of the common ancestor of the haemostatic vitamin-K-dependent serine proteinases

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 7; BLOOD CLOTTING FACTOR 9; COMPLEMENTARY DNA; PROTEIN C; PROTHROMBIN; SERINE PROTEINASE; VITAMIN K GROUP;

EID: 0029737765     PISSN: 03406717     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004390050222     Document Type: Article
Times cited : (14)

References (65)
  • 1
    • 0027288125 scopus 로고
    • Structures of the non-covalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin
    • Arni RK, Padmanabhan K, Padmanabhan KP, Wu TP, Tulinsky A (1993) Structures of the non-covalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin. Biochemistry 32:4727-4737
    • (1993) Biochemistry , vol.32 , pp. 4727-4737
    • Arni, R.K.1    Padmanabhan, K.2    Padmanabhan, K.P.3    Wu, T.P.4    Tulinsky, A.5
  • 2
    • 0026606829 scopus 로고
    • Partial characterization of vertebrate prothrombin cDNAs: Amplification and sequence analysis of the B chain of thrombin from nine different species
    • Banfield DK, MacGillivray RTA (1992) Partial characterization of vertebrate 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    MacGillivray, R.T.A.2
  • 3
    • 0022432305 scopus 로고
    • The structure and evolution of a 461 amino acid human protein C precursor and its messenger RNA, based upon the DNA sequence of cloned human liver cDNAs
    • Beckmann RJ, Schmidt RJ, Santerre RF, Plutzky J, Crabtree GR, Long GL (1985) The structure and evolution of a 461 amino acid human protein C precursor and its messenger RNA, based upon the DNA sequence of cloned human liver cDNAs. Nucleic Acids Res 13:5233-5247
    • (1985) Nucleic Acids Res , vol.13 , pp. 5233-5247
    • Beckmann, R.J.1    Schmidt, R.J.2    Santerre, R.F.3    Plutzky, J.4    Crabtree, G.R.5    Long, G.L.6
  • 7
    • 0028940587 scopus 로고
    • Gene number, noise reduction and biological complexity
    • Bird AP (1995) Gene number, noise reduction and biological complexity. Trends Genet 11:94-100
    • (1995) Trends Genet , vol.11 , pp. 94-100
    • Bird, A.P.1
  • 8
    • 0023512580 scopus 로고
    • Exon and domain evolution in the proenzymes of blood coagulation and fibrinolysis
    • Blake CCF, Harlos K, Holland SK (1987) Exon and domain evolution in the proenzymes of blood coagulation and fibrinolysis. Cold Spring Harb Symp Quant Biol 52:925-931
    • (1987) Cold Spring Harb Symp Quant Biol , vol.52 , pp. 925-931
    • Blake, C.C.F.1    Harlos, K.2    Holland, S.K.3
  • 9
    • 0027050807 scopus 로고
    • The refined 1.9 Å X-ray 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 1.9 Å X-ray 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
  • 10
    • 0025948892 scopus 로고
    • Missense mutations and evolutionary conservation of amino acids: Evidence that many of the amino acids in factor IX function as "spacer" elements
    • Bottema CDK, Ketterling RP, Setsuko L, Yoon H-S, Phillips JA, Sommer SS (1991) Missense mutations and evolutionary conservation of amino acids: evidence that many of the amino acids in factor IX function as "spacer" elements. Am J Hum Genet 49:820-838
    • (1991) Am J Hum Genet , vol.49 , pp. 820-838
    • Bottema, C.D.K.1    Ketterling, R.P.2    Setsuko, L.3    Yoon, H.-S.4    Phillips, J.A.5    Sommer, S.S.6
  • 11
    • 0022534918 scopus 로고
    • Rates of DNA sequence evolution differ between taxonomic groups
    • Britten RJ (1986) Rates of DNA sequence evolution differ between taxonomic groups. Science 231:1393-1398
    • (1986) Science , vol.231 , pp. 1393-1398
    • Britten, R.J.1
  • 12
    • 0027400886 scopus 로고
    • Complete nucleotide sequence of the cDNA encoding rabbit coagulation factor VII
    • Brothers AB, Clarke BJ, Sheffield WP, Blajchman MA (1993) Complete nucleotide sequence of the cDNA encoding rabbit coagulation factor VII. Thromb Res 69:231-238
    • (1993) Thromb Res , vol.69 , pp. 231-238
    • Brothers, A.B.1    Clarke, B.J.2    Sheffield, W.P.3    Blajchman, M.A.4
  • 13
    • 0028343610 scopus 로고
    • Rates of transition and transversion in coding sequences since the human-rodent divergence
    • Collins DW, Jukes TH (1994) Rates of transition and transversion in coding sequences since the human-rodent divergence. Genomics 20:386-396
    • (1994) Genomics , vol.20 , pp. 386-396
    • Collins, D.W.1    Jukes, T.H.2
  • 15
    • 0024382970 scopus 로고
    • Functional evolutionary divergence of proteolytic enzymes and their inhibitors
    • Creighton TE, Darby NJ (1989) Functional evolutionary divergence of proteolytic enzymes and their inhibitors. Trends Biochem Sci 14:319-324
    • (1989) Trends Biochem Sci , vol.14 , pp. 319-324
    • Creighton, T.E.1    Darby, N.J.2
  • 16
    • 0020584329 scopus 로고
    • Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin
    • Degen SJF, MacGillivray RTA, Davie EW (1983) Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin. Biochemistry 22:2087-2097
    • (1983) Biochemistry , vol.22 , pp. 2087-2097
    • Degen, S.J.F.1    MacGillivray, R.T.A.2    Davie, E.W.3
  • 18
    • 0026616336 scopus 로고
    • DNA sequences from a fossil termite in Oligo-Miocene amber and their phylogenetic implications
    • DeSalle R, Gatesy J, Wheeler W, Grimaldi D (1992) DNA sequences from a fossil termite in Oligo-Miocene amber and their phylogenetic implications. Science 257:1933-1936
    • (1992) Science , vol.257 , pp. 1933-1936
    • DeSalle, R.1    Gatesy, J.2    Wheeler, W.3    Grimaldi, D.4
  • 19
  • 20
    • 0027320399 scopus 로고
    • The evolution of vertebrate blood coagulation: A case of Yin and Yang
    • Doolittle RF (1993) The evolution of vertebrate blood coagulation: a case of Yin and Yang. Thromb Haemost 70:24-28
    • (1993) Thromb Haemost , vol.70 , pp. 24-28
    • Doolittle, R.F.1
  • 21
    • 0023512935 scopus 로고
    • Reconstructing the evolution of vertebrate blood coagulation from a consideration of the amino acid sequences of clotting proteins
    • Doolittle RF, Feng DF (1987) Reconstructing the evolution of vertebrate blood coagulation from a consideration of the amino acid sequences of clotting proteins. Cold Spring Harb Symp Quant Biol 52:869-874
    • (1987) Cold Spring Harb Symp Quant Biol , vol.52 , pp. 869-874
    • Doolittle, R.F.1    Feng, D.F.2
  • 24
    • 0014211361 scopus 로고
    • Construction of phylogenetic trees
    • Fitch WM, Margoliash E (1967) Construction of phylogenetic trees. Science 155:279-284
    • (1967) Science , vol.155 , pp. 279-284
    • Fitch, W.M.1    Margoliash, E.2
  • 25
    • 0028976103 scopus 로고
    • Ribosomal DNA phylogeny of the major extant arthropod classes and the evolution of myriapods
    • Friedrich M, Tautz D (1995) Ribosomal DNA phylogeny of the major extant arthropod classes and the evolution of myriapods. Nature 376:165-167
    • (1995) Nature , vol.376 , pp. 165-167
    • Friedrich, M.1    Tautz, D.2
  • 26
    • 0021760465 scopus 로고
    • Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence
    • Fung MR, Campbell RM, MacGillivray RTA (1984) Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence. Nucleic Acids Res 12: 4481-4492
    • (1984) Nucleic Acids Res , vol.12 , pp. 4481-4492
    • Fung, M.R.1    Campbell, R.M.2    MacGillivray, R.T.A.3
  • 27
    • 0028782092 scopus 로고
    • Molecular evolution of serine protease and its inhibitor with special reference to domain evolution
    • Gojobori T, Ikeo K (1994) Molecular evolution of serine protease and its inhibitor with special reference to domain evolution. Philos Trans R Soc Lond Biol 344:411-415
    • (1994) Philos Trans R Soc Lond Biol , vol.344 , pp. 411-415
    • Gojobori, T.1    Ikeo, K.2
  • 28
    • 0020484488 scopus 로고
    • An improved algorithm for matching biological sequences
    • Gotoh O (1982) An improved algorithm for matching biological sequences. J Mol Biol 162:705-708
    • (1982) J Mol Biol , vol.162 , pp. 705-708
    • Gotoh, O.1
  • 29
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of the mammalian serine proteases
    • Greer J (1990) Comparative modeling methods: application to the family of the mammalian serine proteases. Proteins Struc Function Genet 7:317-334
    • (1990) Proteins Struc Function Genet , vol.7 , pp. 317-334
    • Greer, J.1
  • 32
    • 0023188637 scopus 로고
    • Accelerated evolution in the reactive centre regions of serine protease inhibitors
    • Hill RE, Hustie ND (1987) Accelerated evolution in the reactive centre regions of serine protease inhibitors. Nature 326:96-99
    • (1987) Nature , vol.326 , pp. 96-99
    • Hill, R.E.1    Hustie, N.D.2
  • 33
    • 0028895702 scopus 로고
    • Reconstructing the evolutionary history of the artiodactyl ribonuclease superfamily
    • Jermann TM, Opitz JG, Stackhouse J, Benner SA (1995) Reconstructing the evolutionary history of the artiodactyl ribonuclease superfamily. Nature 374:57-59
    • (1995) Nature , vol.374 , pp. 57-59
    • Jermann, T.M.1    Opitz, J.G.2    Stackhouse, J.3    Benner, S.A.4
  • 34
    • 0000732090 scopus 로고
    • Evolution of protein molecules
    • Munro HN (ed) Academic Press, New York
    • Jukes TH, Cantor CR (1969) Evolution of protein molecules. In: Munro HN (ed) Mammalian protein metabolism. Academic Press, New York, pp 21-132
    • (1969) Mammalian Protein Metabolism , pp. 21-132
    • Jukes, T.H.1    Cantor, C.R.2
  • 36
    • 0029941720 scopus 로고    scopus 로고
    • Single base-pair substitutions in pathology and evolution: Two sides to the same coin
    • Krawczak M, Cooper DN (1996) Single base-pair substitutions in pathology and evolution: two sides to the same coin. Hum Mutat 8:23-31
    • (1996) Hum Mutat , vol.8 , pp. 23-31
    • Krawczak, M.1    Cooper, D.N.2
  • 37
    • 0022871419 scopus 로고
    • Gene for human factor X: A blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C
    • Leytus SP, Foster DC, Kurachi K, Davie EW (1986) Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry 25:5098-5102
    • (1986) Biochemistry , vol.25 , pp. 5098-5102
    • Leytus, S.P.1    Foster, D.C.2    Kurachi, K.3    Davie, E.W.4
  • 38
  • 39
    • 0021759451 scopus 로고
    • Characterization of bovine prothrombin mRNA and its translation product
    • MacGillivray RTA, Davie EW (1984) Characterization of bovine prothrombin mRNA and its translation product. Biochemistry 23:1626-1634
    • (1984) Biochemistry , vol.23 , pp. 1626-1634
    • MacGillivray, R.T.A.1    Davie, E.W.2
  • 40
    • 0025270813 scopus 로고
    • Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing
    • Malcolm BA, Wilson KP, Matthews BW, Kirsch JF, Wilson AC (1990) Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing. Nature 345:86-89
    • (1990) Nature , vol.345 , pp. 86-89
    • Malcolm, B.A.1    Wilson, K.P.2    Matthews, B.W.3    Kirsch, J.F.4    Wilson, A.C.5
  • 41
    • 0026767457 scopus 로고
    • Liver-specific expression of the gene coding for human factor X, a blood coagulation factor
    • Miao CH, Leytus SP, Chung DW, Davie EW (1992) Liver-specific expression of the gene coding for human factor X, a blood coagulation factor. J Biol Chem 267:7395-7401
    • (1992) J Biol Chem , vol.267 , pp. 7395-7401
    • Miao, C.H.1    Leytus, S.P.2    Chung, D.W.3    Davie, E.W.4
  • 43
    • 0028357936 scopus 로고
    • Analysis of the partial nucleotide sequences and deduced primary structures of the protease domains of mammalian blood coagulation factors VII and X
    • Murakawa M, Okamura T, Kamara T, Kuroiwa M, Harada M, Niho Y (1994a) Analysis of the partial nucleotide sequences and deduced primary structures of the protease domains of mammalian blood coagulation factors VII and X. Eur J Haematol 52:162-168
    • (1994) Eur J Haematol , vol.52 , pp. 162-168
    • Murakawa, M.1    Okamura, T.2    Kamara, T.3    Kuroiwa, M.4    Harada, M.5    Niho, Y.6
  • 44
    • 0028361314 scopus 로고
    • A comparative study of partial primary structures of the catalytic region of mammalian protein C
    • Murakawa M, Okamura T, Kamura T, Kuroiwa M, Harada M (1994b) A comparative study of partial primary structures of the catalytic region of mammalian protein C. Br J Haematol 86:590-600
    • (1994) Br J Haematol , vol.86 , pp. 590-600
    • Murakawa, M.1    Okamura, T.2    Kamura, T.3    Kuroiwa, M.4    Harada, M.5
  • 46
    • 0021273620 scopus 로고
    • Evolution of proteolytic enzymes
    • Neurath H (1984) Evolution of proteolytic enzymes. Science 224:350-357
    • (1984) Science , vol.224 , pp. 350-357
    • Neurath, H.1
  • 47
    • 0026557719 scopus 로고
    • Mammalian phylogeny: Shaking the tree
    • Novacek MJ (1992) Mammalian phylogeny: shaking the tree. Nature 356:121-125
    • (1992) Nature , vol.356 , pp. 121-125
    • Novacek, M.J.1
  • 49
    • 0025936264 scopus 로고
    • Multigene families and the evolution of complexity
    • Ohta T (1991) Multigene families and the evolution of complexity. J Mol Evol 33:34-41
    • (1991) J Mol Evol , vol.33 , pp. 34-41
    • Ohta, T.1
  • 50
    • 0028053868 scopus 로고
    • On hypervariability at the reactive center of proteolytic enzymes and their inhibitors
    • Ohta T (1994) On hypervariability at the reactive center of proteolytic enzymes and their inhibitors. J Mol Evol 39:614-619
    • (1994) J Mol Evol , vol.39 , pp. 614-619
    • Ohta, T.1
  • 52
    • 0022102222 scopus 로고
    • Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules
    • Patthy L (1985) Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 41:657-663
    • (1985) Cell , vol.41 , pp. 657-663
    • Patthy, L.1
  • 53
    • 0025142701 scopus 로고
    • Evolutionary assembly of blood coagulation proteins
    • Patthy L (1990) Evolutionary assembly of blood coagulation proteins. Semin Thromb Haemost 16:245-259
    • (1990) Semin Thromb Haemost , vol.16 , pp. 245-259
    • Patthy, L.1
  • 54
    • 0022416122 scopus 로고
    • Exon shuffling and intron insertion in serine protease genes
    • Rogers J (1985) Exon shuffling and intron insertion in serine protease genes. Nature 315:458-459
    • (1985) Nature , vol.315 , pp. 458-459
    • Rogers, J.1
  • 55
    • 0025333881 scopus 로고
    • Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species
    • Sarkar G, Koeberl DD, Sommer SS (1990) Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species. Genomics 6:133-143
    • (1990) Genomics , vol.6 , pp. 133-143
    • Sarkar, G.1    Koeberl, D.D.2    Sommer, S.S.3
  • 57
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • Stubbs MT, Bode W (1993) A player of many parts: the spotlight falls on thrombin's structure. Thromb Res 69:1-58
    • (1993) Thromb Res , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 62
    • 0027311097 scopus 로고
    • A molecular model of the serine protease domain of activated protein C: Application to the study of missense mutations causing protein C deficiency
    • Wacey AI, Pemberton S, Cooper DN, Kakkar VV, Tuddenham EGD (1993) A molecular model of the serine protease domain of activated protein C: application to the study of missense mutations causing protein C deficiency. Br J Haematol 84:290-300
    • (1993) Br J Haematol , vol.84 , pp. 290-300
    • Wacey, A.I.1    Pemberton, S.2    Cooper, D.N.3    Kakkar, V.V.4    Tuddenham, E.G.D.5
  • 63
    • 0028165399 scopus 로고
    • DNA sequence from Cretacious period bone fragments
    • Woodward SR, Weyward NJ, Bunnell M (1994) DNA sequence from Cretacious period bone fragments. Science 266:1229-1232
    • (1994) Science , vol.266 , pp. 1229-1232
    • Woodward, S.R.1    Weyward, N.J.2    Bunnell, M.3
  • 64
    • 0025361521 scopus 로고
    • Deduced amino acid sequence of mouse blood coagulation factor IX
    • Wu SM, Stafford DW, Ware J (1990) Deduced amino acid sequence of mouse blood coagulation factor IX. Gene 86:275-278
    • (1990) Gene , vol.86 , pp. 275-278
    • Wu, S.M.1    Stafford, D.W.2    Ware, J.3
  • 65
    • 0022257323 scopus 로고
    • Nucleotide sequence of the gene for human factor IX (antihemophilic factor B)
    • Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K (1985) Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry 24:3736-3750
    • (1985) Biochemistry , vol.24 , pp. 3736-3750
    • Yoshitake, S.1    Schach, B.G.2    Foster, D.C.3    Davie, E.W.4    Kurachi, K.5


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