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Volumn 366, Issue 2, 2007, Pages 602-610

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

Author keywords

factor VIIa tissue factor complex; factor Xa exosite; inhibition; nematode anticoagulant protein; selectide inhibitor

Indexed keywords

4 CARBOXYGLUTAMIC ACID; ANTICOAGULANT PROTEIN; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 7A; DRUG RESIDUE; FACTOR XA EXOSITE; NAPC2 PROTEIN; POLYPEPTIDE; UNCLASSIFIED DRUG;

EID: 33846377756     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.040     Document Type: Article
Times cited : (39)

References (36)
  • 1
    • 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
  • 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
    • 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
  • 6
    • 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 Hotex 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    Hotex, P.5
  • 8
    • 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) 586-593
    • (1990) Science , vol.248 , pp. 586-593
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 9
    • 0037135531 scopus 로고    scopus 로고
    • Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase
    • Buddai S.K., Toulokhonova L., Bergum P.W., Vlasuk P., and Krishnaswamy S. Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase. J. Biol. Chem. 277 (2002) 26689-26698
    • (2002) J. Biol. Chem. , vol.277 , pp. 26689-26698
    • Buddai, S.K.1    Toulokhonova, L.2    Bergum, P.W.3    Vlasuk, P.4    Krishnaswamy, S.5
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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
  • 22
    • 33751552981 scopus 로고
    • Concerning the thermodynamics of molecular recognition in aqueous and organic media. Evidence for significant heat capacity effects
    • Stauffer D.A., Barrans R.E., and Dougherty D.A. Concerning the thermodynamics of molecular recognition in aqueous and organic media. Evidence for significant heat capacity effects. 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
  • 23
    • 12044251218 scopus 로고
    • Directionality of the cation-π effect: a charge-mediated size selectivity in binding
    • Schwabacher A.W., Zhang S., and Davy W. Directionality of the cation-π 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
  • 24
    • 0028984438 scopus 로고
    • Proposed cation-π mediated binding by factor Xa: a novel enzymatic mechanism for molecular recognition
    • Lim Z., and Johnson M.E. Proposed cation-π mediated binding by factor Xa: a novel enzymatic mechanism for molecular recognition. FEBS Letters 370 (1995) 1-5
    • (1995) FEBS Letters , vol.370 , pp. 1-5
    • Lim, Z.1    Johnson, M.E.2
  • 25
    • 0034005173 scopus 로고    scopus 로고
    • Structure of tick anticoagulant peptide at 1.6 Å resolution complexed with bovine pancreatic trypsin inhibitor
    • St. Charles R., Padmananbhan K., Arni R.K., Padmanabhan K.P., and Tulinsky A. Structure of tick anticoagulant peptide at 1.6 Å resolution complexed with bovine pancreatic trypsin inhibitor. Protein Sci. 9 (2000) 256-272
    • (2000) Protein Sci. , vol.9 , pp. 256-272
    • St. Charles, R.1    Padmananbhan, K.2    Arni, R.K.3    Padmanabhan, K.P.4    Tulinsky, A.5
  • 26
    • 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
  • 27
    • 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
  • 28
    • 77956905650 scopus 로고
    • Pancreatic elastase
    • Boyer P.D. (Ed), Academic Press, New York
    • Harley B.S., and Shotton D.M. Pancreatic elastase. In: Boyer P.D. (Ed). The Enzymes. 1st edit. (1971), Academic Press, New York 323-373
    • (1971) The Enzymes. 1st edit. , pp. 323-373
    • Harley, B.S.1    Shotton, D.M.2
  • 29
    • 0242362193 scopus 로고    scopus 로고
    • The tissue factor/factor VIIa/factor Xa complex: a model built by docking and site-directed mutagenesis
    • Norledge B.V., Petrovan R.J., Ruf W., and Olson A.J. The tissue factor/factor VIIa/factor Xa complex: a model built by docking and site-directed mutagenesis. Proteins: Struct. Funct. Genet. 53 (2003) 640-648
    • (2003) Proteins: Struct. Funct. Genet. , vol.53 , pp. 640-648
    • Norledge, B.V.1    Petrovan, R.J.2    Ruf, W.3    Olson, A.J.4
  • 30
    • 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
  • 31
    • 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
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collection in oscillation mode
    • Otwinoski Z., and Minor W. Processing of X-ray diffraction data collection in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinoski, Z.1    Minor, W.2
  • 33
    • 0000997620 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. D 49 (1993) 588-591
    • (1993) Acta Crystallog. sect. D , vol.49 , pp. 588-591
    • Navaza, J.1
  • 34
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 36
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thorton 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    Thorton, J.M.4


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