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Volumn 371, Issue 3, 2007, Pages 774-786

Active and Exo-site Inhibition of Human Factor Xa: Structure of des-Gla Factor Xa Inhibited by NAP5, a Potent Nematode Anticoagulant Protein from Ancylostoma caninum

Author keywords

active and exo site binding; factor X Xa; ixolaris; nematode anticoagulant proteins; tissue factor pathway inhibitor

Indexed keywords

4 CARBOXYGLUTAMIC ACID; ANTICOAGULANT PROTEIN; BLOOD CLOTTING FACTOR 10; DISULFIDE; ELASTASE; NAP5 PROTEIN; TISSUE FACTOR PATHWAY INHIBITOR; UNCLASSIFIED DRUG;

EID: 34447640731     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.05.042     Document Type: Article
Times cited : (26)

References (64)
  • 1
    • 0026337077 scopus 로고
    • The coagulation cascade: initiation, maintenance, and regulation
    • Davie E.W., Fujikawa K., and Kisiel W. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 30 (1991) 10363-10370
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 2
    • 0021891883 scopus 로고
    • Vitamin K-dependent carboxylase
    • Suttie J.W. Vitamin K-dependent carboxylase. Annu. Rev. Biochem. 54 (1985) 459-477
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 459-477
    • Suttie, J.W.1
  • 3
    • 0020966026 scopus 로고
    • Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid
    • McMullen B.A., Fujikawa K., Kisiel W., Sasagawa T., Howald W.N., Kwa E.Y., and Weinstein B. Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid. Biochemistry 22 (1983) 2875-2884
    • (1983) Biochemistry , vol.22 , pp. 2875-2884
    • McMullen, B.A.1    Fujikawa, K.2    Kisiel, W.3    Sasagawa, T.4    Howald, W.N.5    Kwa, E.Y.6    Weinstein, B.7
  • 4
    • 0021112692 scopus 로고
    • Beta-hydroxyaspartic acid in vitamin K-dependent proteins
    • Fernlund P., and Stenflo J. Beta-hydroxyaspartic acid in vitamin K-dependent proteins. J. Biol. Chem. 258 (1983) 12509-12512
    • (1983) J. Biol. Chem. , vol.258 , pp. 12509-12512
    • Fernlund, P.1    Stenflo, J.2
  • 5
    • 0017762527 scopus 로고
    • Activation of human factor X (Stuart factor) by a protease from Russell's viper venom
    • DiScipio R.G., Hermodson M.A., and Davie E.W. Activation of human factor X (Stuart factor) by a protease from Russell's viper venom. Biochemistry 16 (1977) 5253-5260
    • (1977) Biochemistry , vol.16 , pp. 5253-5260
    • DiScipio, R.G.1    Hermodson, M.A.2    Davie, E.W.3
  • 6
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann K.G., Nesheim M.E., Church W.R., Haley P., and Krishnaswamy S. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood 76 (1990) 1-16
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 7
    • 28244481846 scopus 로고    scopus 로고
    • Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator
    • Murakami M.T., and Arni R.K. Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator. J. Biol. Chem. 280 (2005) 39015-39309
    • (2005) J. Biol. Chem. , vol.280 , pp. 39015-39309
    • Murakami, M.T.1    Arni, R.K.2
  • 8
    • 0032530323 scopus 로고    scopus 로고
    • The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases
    • Parry M.A., Jacob U., Huber R., Wisner A., Bon C., and Bode W. The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases. Structure 6 (1998) 1195-1206
    • (1998) Structure , vol.6 , pp. 1195-1206
    • Parry, M.A.1    Jacob, U.2    Huber, R.3    Wisner, A.4    Bon, C.5    Bode, W.6
  • 9
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman L., Smith D.E., Arcuri K.E., and Vlasuk G.P. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 248 (1990) 593-596
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 10
    • 0029014045 scopus 로고
    • Ancylostoma caninum anticoagulant peptide: a hookworm-derived inhibitor of human coagulation factor Xa
    • Cappello M., Vlasuk G.P., Bergum P.W., Huang S., and Hotez P. Ancylostoma caninum anticoagulant peptide: a hookworm-derived inhibitor of human coagulation factor Xa. Proc. Natl Acad. Sci. USA 92 (1995) 6152-6156
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6152-6156
    • Cappello, M.1    Vlasuk, G.P.2    Bergum, P.W.3    Huang, S.4    Hotez, P.5
  • 12
    • 0013965976 scopus 로고
    • The nature and causes of "hookworm anemia"
    • Roche M., and Layrisse M. The nature and causes of "hookworm anemia". Am. J. Trop. Med. Hyg. 15 (1966) 1029-1102
    • (1966) Am. J. Trop. Med. Hyg. , vol.15 , pp. 1029-1102
    • Roche, M.1    Layrisse, M.2
  • 13
    • 0030856003 scopus 로고    scopus 로고
    • Antithrombotic efficacy of a recombinant nematode anticoagulant peptide (rNAP5) in canine models of thrombosis after single subcutaneous administration
    • Rebello S.S., Blank H.S., Rote W.F., Vlasuk G.P., and Lucchesi B.R. Antithrombotic efficacy of a recombinant nematode anticoagulant peptide (rNAP5) in canine models of thrombosis after single subcutaneous administration. J. Pharmacol. Expt. Ther. 283 (1997) 91-99
    • (1997) J. Pharmacol. Expt. Ther. , vol.283 , pp. 91-99
    • Rebello, S.S.1    Blank, H.S.2    Rote, W.F.3    Vlasuk, G.P.4    Lucchesi, B.R.5
  • 14
    • 33846377756 scopus 로고    scopus 로고
    • Intermolecular interactions and characterization of the novel factor Xa exosite involved in macromolecular recognition and inhibition: crystal structure of human Gla-domainless factor Xa complexed with the anticoagulant protein napc2 from the hematophagous nematode Ancylostoma caninum
    • Murakami M.T., Rios-Steiner J., Weaver S.E., Tulinsky A., Geiger J.H., and Arni R.K. Intermolecular interactions and characterization of the novel factor Xa exosite involved in macromolecular recognition and inhibition: crystal structure of human Gla-domainless factor Xa complexed with the anticoagulant protein napc2 from the hematophagous nematode Ancylostoma caninum. J. Mol. Biol. 366 (2007) 602-610
    • (2007) J. Mol. Biol. , vol.366 , pp. 602-610
    • Murakami, M.T.1    Rios-Steiner, J.2    Weaver, S.E.3    Tulinsky, A.4    Geiger, J.H.5    Arni, R.K.6
  • 15
    • 0021453880 scopus 로고
    • The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the primary structure
    • Babin D.R., Peanasky R.J., and Goos S.M. The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the primary structure. Arch. Biochem. Biophys. 232 (1984) 143-161
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 143-161
    • Babin, D.R.1    Peanasky, R.J.2    Goos, S.M.3
  • 16
    • 0028773904 scopus 로고
    • High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site
    • Grasberger B.L., Clore G.M., and Gronenborn A.M. High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site. Structure 2 (1994) 669-678
    • (1994) Structure , vol.2 , pp. 669-678
    • Grasberger, B.L.1    Clore, G.M.2    Gronenborn, A.M.3
  • 17
    • 0028773905 scopus 로고
    • The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase
    • Huang K., Strynadka N.C.J., Bernard V.D., Peanasky R.J., and James M.N.G. The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure 2 (1994) 679-689
    • (1994) Structure , vol.2 , pp. 679-689
    • Huang, K.1    Strynadka, N.C.J.2    Bernard, V.D.3    Peanasky, R.J.4    James, M.N.G.5
  • 18
    • 0033599835 scopus 로고    scopus 로고
    • Thrombosis: new antithrombotic agents
    • Hirsh J., and Weitz J.I. Thrombosis: new antithrombotic agents. Lancet 353 (1999) 1431-1436
    • (1999) Lancet , vol.353 , pp. 1431-1436
    • Hirsh, J.1    Weitz, J.I.2
  • 19
    • 0030858230 scopus 로고    scopus 로고
    • Low molecular weight heparins
    • Weitz J.I. Low molecular weight heparins. N. Engl. J. Med. 337 (1997) 688-698
    • (1997) N. Engl. J. Med. , vol.337 , pp. 688-698
    • Weitz, J.I.1
  • 20
    • 0035912739 scopus 로고    scopus 로고
    • Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X
    • Mizuno H., Fujimoto Z., Atoda H., and Morita T. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc. Natl Acad. Sci. USA 98 (2001) 7230-7234
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7230-7234
    • Mizuno, H.1    Fujimoto, Z.2    Atoda, H.3    Morita, T.4
  • 22
    • 0037093065 scopus 로고    scopus 로고
    • Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex
    • Francischetti I.M., Valenzuela J.G., Andersen J.F., Mather T.N., and Ribeiro J.M. Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex. Blood 99 (2002) 3602-3612
    • (2002) Blood , vol.99 , pp. 3602-3612
    • Francischetti, I.M.1    Valenzuela, J.G.2    Andersen, J.F.3    Mather, T.N.4    Ribeiro, J.M.5
  • 24
    • 0029923976 scopus 로고    scopus 로고
    • X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition
    • Brandstetter H., Kuhne A., Bode W., Huber R., von der Saal W., Wirthensohn K., and Engh R.A. X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition. J. Biol. Chem. 271 (1996) 29988-29992
    • (1996) J. Biol. Chem. , vol.271 , pp. 29988-29992
    • Brandstetter, H.1    Kuhne, A.2    Bode, W.3    Huber, R.4    von der Saal, W.5    Wirthensohn, K.6    Engh, R.A.7
  • 25
    • 0032538320 scopus 로고    scopus 로고
    • Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa
    • Wei A., Alexander R.S., Duke J., Ross H., Rosenfeld S.A., and Chang C.-H. Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J. Mol. Biol. 283 (1998) 147-154
    • (1998) J. Mol. Biol. , vol.283 , pp. 147-154
    • Wei, A.1    Alexander, R.S.2    Duke, J.3    Ross, H.4    Rosenfeld, S.A.5    Chang, C.-H.6
  • 26
    • 0032499683 scopus 로고    scopus 로고
    • Structural basis for chemical inhibition of human blood coagulation factor Xa
    • Kamata K., Kawamoto H., Honma T., Iwama T., and Kim S.-H. Structural basis for chemical inhibition of human blood coagulation factor Xa. Proc. Natl Acad. Sci. USA 95 (1998) 6630-6635
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6630-6635
    • Kamata, K.1    Kawamoto, H.2    Honma, T.3    Iwama, T.4    Kim, S.-H.5
  • 27
    • 0017802964 scopus 로고
    • The effect of metal ions on the amidolytic acitivity of human factor Xa (activated Stuart-Prower factor)
    • Orthner C.L., and Kosow D.P. The effect of metal ions on the amidolytic acitivity of human factor Xa (activated Stuart-Prower factor). Arch. Biochem. Biophys. 185 (1978) 400-406
    • (1978) Arch. Biochem. Biophys. , vol.185 , pp. 400-406
    • Orthner, C.L.1    Kosow, D.P.2
  • 28
    • 0019255615 scopus 로고
    • Evidence that human alpha-thrombin is a monovalent cation-activated enzyme
    • Orthner C.L., and Kosow D.P. Evidence that human alpha-thrombin is a monovalent cation-activated enzyme. Arch. Biochem. Biophys. 202 (1980) 63-75
    • (1980) Arch. Biochem. Biophys. , vol.202 , pp. 63-75
    • Orthner, C.L.1    Kosow, D.P.2
  • 29
    • 0019324165 scopus 로고
    • Stimulation of the amidase and esterase activity of activated bovine plasma protein C by monovalent cations
    • Steiner S.A., Amphlett G.N., and Castellino F.J. Stimulation of the amidase and esterase activity of activated bovine plasma protein C by monovalent cations. Biochem. Biophys. Res. Commun. 94 (1980) 340-347
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 340-347
    • Steiner, S.A.1    Amphlett, G.N.2    Castellino, F.J.3
  • 30
    • 0030935412 scopus 로고    scopus 로고
    • The molecular environment of the Na+ binding site of thrombin
    • Zhang E., and Tulinsky A. The molecular environment of the Na+ binding site of thrombin. Biophys. Chem. 63 (1997) 185-200
    • (1997) Biophys. Chem. , vol.63 , pp. 185-200
    • Zhang, E.1    Tulinsky, A.2
  • 31
    • 0027340393 scopus 로고
    • Effects of Ca2+ binding on the protease module of factor Xa and its interaction with factor Va. Evidence for two Gla-independent Ca(2+)-binding sites in factor Xa
    • Persson E., Hogg P.J., and Senflo J. Effects of Ca2+ binding on the protease module of factor Xa and its interaction with factor Va. Evidence for two Gla-independent Ca(2+)-binding sites in factor Xa. J. Biol. Chem. 268 (1993) 22531-22539
    • (1993) J. Biol. Chem. , vol.268 , pp. 22531-22539
    • Persson, E.1    Hogg, P.J.2    Senflo, J.3
  • 33
    • 0026502691 scopus 로고
    • Antibody-probed conformational transitions in the protease domain of human factor IX upon calcium binding and zymogen activation: putative high-affinity Ca(2+)-binding site in the protease domain
    • Bajaj S.P., Sabharwal A.K., Gorka J., and Birktoft J.J. Antibody-probed conformational transitions in the protease domain of human factor IX upon calcium binding and zymogen activation: putative high-affinity Ca(2+)-binding site in the protease domain. Proc. Natl Acad. Sci. USA 89 (1992) 152-156
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 152-156
    • Bajaj, S.P.1    Sabharwal, A.K.2    Gorka, J.3    Birktoft, J.J.4
  • 34
    • 0016796849 scopus 로고
    • The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0
    • Bode W., and Schwager P. The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J. Mol. Biol. 98 (1975) 693-717
    • (1975) J. Mol. Biol. , vol.98 , pp. 693-717
    • Bode, W.1    Schwager, P.2
  • 35
    • 0029965611 scopus 로고    scopus 로고
    • Crystal structures of thrombin with thiazole-containing inhibitors: probes of the S1′ binding site
    • Matthews J.H., Krishnan R., Costanzo M.J., Maryanoff B.E., and Tulinsky A. Crystal structures of thrombin with thiazole-containing inhibitors: probes of the S1′ binding site. Biophys. J. 71 (1996) 2830-2839
    • (1996) Biophys. J. , vol.71 , pp. 2830-2839
    • Matthews, J.H.1    Krishnan, R.2    Costanzo, M.J.3    Maryanoff, B.E.4    Tulinsky, A.5
  • 36
    • 0033594326 scopus 로고    scopus 로고
    • Bound structures of novel P3-P1′ beta-strand mimetic inhibitors of thrombin
    • St. Charles R., Matthews J.H., Zhang E., and Tulinsky A. Bound structures of novel P3-P1′ beta-strand mimetic inhibitors of thrombin. J. Med. Chem. 42 (1999) 1376-1383
    • (1999) J. Med. Chem. , vol.42 , pp. 1376-1383
    • St. Charles, R.1    Matthews, J.H.2    Zhang, E.3    Tulinsky, A.4
  • 37
    • 0023657928 scopus 로고
    • The geometries of interacting arginine-carboxyls in proteins
    • Singh J., Thornton J.M., Snarey M., and Campbell S.F. The geometries of interacting arginine-carboxyls in proteins. FEBS Letters 224 (1987) 161-171
    • (1987) FEBS Letters , vol.224 , pp. 161-171
    • Singh, J.1    Thornton, J.M.2    Snarey, M.3    Campbell, S.F.4
  • 39
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., and Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204 (1992) 433-451
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 40
    • 0029985841 scopus 로고    scopus 로고
    • Comparison of the structures of the cyclotheonamide A complexes of human alpha-thrombin and bovine beta-trypsin
    • Ganesh V., Lee A.Y., Clardy J., and Tulinsky A. Comparison of the structures of the cyclotheonamide A complexes of human alpha-thrombin and bovine beta-trypsin. Protein Sci. 5 (1996) 825-835
    • (1996) Protein Sci. , vol.5 , pp. 825-835
    • Ganesh, V.1    Lee, A.Y.2    Clardy, J.3    Tulinsky, A.4
  • 41
    • 0032167901 scopus 로고    scopus 로고
    • Highly selective mechanism-based thrombin inhibitors: structures of thrombin and trypsin inhibited with rigid peptidyl aldehydes
    • Krishnan R., Zhang E., Hakansson K., Arni R.K., Tulinsky A., Lim-Wilby M.S.L., et al. Highly selective mechanism-based thrombin inhibitors: structures of thrombin and trypsin inhibited with rigid peptidyl aldehydes. Biochemistry 37 (1998) 12094-12103
    • (1998) Biochemistry , vol.37 , pp. 12094-12103
    • Krishnan, R.1    Zhang, E.2    Hakansson, K.3    Arni, R.K.4    Tulinsky, A.5    Lim-Wilby, M.S.L.6
  • 42
    • 0025675821 scopus 로고
    • Acetylcholine binding by a synthetic receptor: implications for biological recognition
    • Dougherty D.A., and Stauffer D.A. Acetylcholine binding by a synthetic receptor: implications for biological recognition. Science 250 (1990) 1558-1560
    • (1990) Science , vol.250 , pp. 1558-1560
    • Dougherty, D.A.1    Stauffer, D.A.2
  • 43
    • 33751552981 scopus 로고
    • Concerning the thermodynamics of molecular recognition in aqueous and organic media
    • Stauffer D.A., Barrans R.E., and Dougherty D.A. Concerning the thermodynamics of molecular recognition in aqueous and organic media. J. Org. Chem. 55 (1990) 2762-2767
    • (1990) J. Org. Chem. , vol.55 , pp. 2762-2767
    • Stauffer, D.A.1    Barrans, R.E.2    Dougherty, D.A.3
  • 44
    • 12044251218 scopus 로고
    • Directionality of the cation-p effect: a charge-mediated size selectivity in binding
    • Schwabacher A.W., Zhang S., and Davy W. Directionality of the cation-p effect: a charge-mediated size selectivity in binding. J. Am. Chem. Soc. 115 (1993) 6995-6996
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6995-6996
    • Schwabacher, A.W.1    Zhang, S.2    Davy, W.3
  • 45
    • 0033118633 scopus 로고    scopus 로고
    • Structures of thrombin retro-inhibited with SEL2711 and SEL2770 as they relate to factor Xa binding
    • Mochalkin I., and Tulinsky A. Structures of thrombin retro-inhibited with SEL2711 and SEL2770 as they relate to factor Xa binding. Acta Crystallog. sect. D 55 (1999) 785-793
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 785-793
    • Mochalkin, I.1    Tulinsky, A.2
  • 47
    • 0016291686 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution
    • Huber R., Kukla D., Bode W., Schwager P., Bartels K., Deisenhofer J., and Steigemann W. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution. J. Mol. Biol. 89 (1974) 73-101
    • (1974) J. Mol. Biol. , vol.89 , pp. 73-101
    • Huber, R.1    Kukla, D.2    Bode, W.3    Schwager, P.4    Bartels, K.5    Deisenhofer, J.6    Steigemann, W.7
  • 48
    • 0033569932 scopus 로고    scopus 로고
    • Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2
    • Duggan B.M., Dyson H.J., and Wright P.E. Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2. Eur. J. Biochem. 265 (1999) 539-548
    • (1999) Eur. J. Biochem. , vol.265 , pp. 539-548
    • Duggan, B.M.1    Dyson, H.J.2    Wright, P.E.3
  • 49
    • 0022979292 scopus 로고
    • Preparation and properties of derivatives of bovine factor X and factor Xa from which the gamma-carboxyglutamic acid containing domain has been removed
    • Morita T., and Jackson C.M. Preparation and properties of derivatives of bovine factor X and factor Xa from which the gamma-carboxyglutamic acid containing domain has been removed. J. Biol. Chem. 261 (1986) 4015-4023
    • (1986) J. Biol. Chem. , vol.261 , pp. 4015-4023
    • Morita, T.1    Jackson, C.M.2
  • 50
    • 0028081167 scopus 로고
    • High-level secretion and very efficient isotopic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Pichia pastoris
    • Laroche Y., Storme V., De Meutter I., Messens J., and Lauwereys M. High-level secretion and very efficient isotopic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Pichia pastoris. BioTechnology 12 (1994) 1119-1124
    • (1994) BioTechnology , vol.12 , pp. 1119-1124
    • Laroche, Y.1    Storme, V.2    De Meutter, I.3    Messens, J.4    Lauwereys, M.5
  • 51
    • 0026206788 scopus 로고
    • Sparse matrix sampling: a screening method for crystallization of proteins
    • Jancarik H., and Kim S.H. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallog. 24 (1991) 409-411
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 409-411
    • Jancarik, H.1    Kim, S.H.2
  • 53
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 54
    • 0000997620 scopus 로고
    • On the computation of the fast rotation function
    • Navaza J. On the computation of the fast rotation function. Acta Crystallog. sect. D 49 (1993) 588-591
    • (1993) Acta Crystallog. sect. D , vol.49 , pp. 588-591
    • Navaza, J.1
  • 56
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO in
    • Jones T.A. Interactive computer graphics: FRODO in. Metodhs Enzymol. 115 (1985) 157-171
    • (1985) Metodhs Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 57
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 58
    • 0034602930 scopus 로고    scopus 로고
    • High resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence
    • Czapinska H., Otlewski J., Krzywda S., Sheldrick G.M., and Jaskolski M. High resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence. J. Mol. Biol. 295 (2000) 1237-1249
    • (2000) J. Mol. Biol. , vol.295 , pp. 1237-1249
    • Czapinska, H.1    Otlewski, J.2    Krzywda, S.3    Sheldrick, G.M.4    Jaskolski, M.5
  • 59
    • 0031566430 scopus 로고    scopus 로고
    • The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa
    • Burgering M.J., Orbons L.P., van der Doelen A., Mulders J., Theunissen H.J., Grootenhuis P.D., et al. The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa. J. Mol. Biol. 269 (1997) 395-407
    • (1997) J. Mol. Biol. , vol.269 , pp. 395-407
    • Burgering, M.J.1    Orbons, L.P.2    van der Doelen, A.3    Mulders, J.4    Theunissen, H.J.5    Grootenhuis, P.D.6
  • 60
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: generation and refinement of homology-based protein struture models
    • Fiser A., and Sali A. Modeller: generation and refinement of homology-based protein struture models. Methods Enzymol. 374 (2003) 461-491
    • (2003) Methods Enzymol. , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 61
    • 0346882663 scopus 로고    scopus 로고
    • ModLoop: automated modeling of loops in protein structures
    • Fiser A., and Sali A. ModLoop: automated modeling of loops in protein structures. Bioinformatics 19 (2003) 2500-2501
    • (2003) Bioinformatics , vol.19 , pp. 2500-2501
    • Fiser, A.1    Sali, A.2
  • 62
    • 0035789518 scopus 로고    scopus 로고
    • Gromacs 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., and van der Spoe D.L. Gromacs 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Mod. 7 (2001) 306-317
    • (2001) J. Mol. Mod. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoe, D.L.3
  • 63
    • 0030767485 scopus 로고    scopus 로고
    • VEFIY3D: assessment of protein models with three-dimensional profiles
    • Eisenberg D., Luthy R., and Bowie J.U. VEFIY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol. 277 (1997) 396-404
    • (1997) Methods Enzymol. , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 64
    • 0033524955 scopus 로고    scopus 로고
    • Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant
    • Zhang E., St Charles R., and Tulinsky A. Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant. J. Mol. Biol. 285 (1999) 2089-2104
    • (1999) J. Mol. Biol. , vol.285 , pp. 2089-2104
    • Zhang, E.1    St Charles, R.2    Tulinsky, A.3


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