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Volumn 357, Issue 1, 2006, Pages 195-209

X-ray structures of free and leupeptin-complexed human αI-tryptase mutants: Indication for an α→β-tryptase transition

Author keywords

Active site flexibility; Asthma; Trypsin like serine proteinase; Tryptase; X ray crystallography

Indexed keywords

ALPHA TRYPTASE; AMINO ACID; BETA TRYPTASE; LEUPEPTIN; MONOMER; TETRAMER; TRYPTASE; UNCLASSIFIED DRUG;

EID: 33644776716     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.12.037     Document Type: Article
Times cited : (27)

References (75)
  • 2
    • 0036034837 scopus 로고    scopus 로고
    • New developments in the genetics and activation of mast cell proteases
    • G.H. Caughey New developments in the genetics and activation of mast cell proteases Mol. Immunol. 38 2002 1353 1357
    • (2002) Mol. Immunol. , vol.38 , pp. 1353-1357
    • Caughey, G.H.1
  • 3
    • 3042615524 scopus 로고    scopus 로고
    • Mast cell tryptase, a still enigmatic enzyme
    • L. Fiorucci, and F. Ascoli Mast cell tryptase, a still enigmatic enzyme Cell Mol. Life Sci. 61 2004 1278 1295
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 1278-1295
    • Fiorucci, L.1    Ascoli, F.2
  • 4
    • 0030068941 scopus 로고    scopus 로고
    • A novel heparin-dependent processing pathway for human tryptase-autocatalysis followed by activation with dipeptidyl peptidase I
    • K. Sakai, S.L. Ren, and L.B. Schwartz A novel heparin-dependent processing pathway for human tryptase-autocatalysis followed by activation with dipeptidyl peptidase I J. Clin. Invest. 97 1996 988 995
    • (1996) J. Clin. Invest. , vol.97 , pp. 988-995
    • Sakai, K.1    Ren, S.L.2    Schwartz, L.B.3
  • 5
    • 9644262525 scopus 로고    scopus 로고
    • Structural requirements and mechanism for heparin-dependent activation and tetramerization of human beta I and beta II-tryptase
    • J. Hallgren, S. Lindahl, and G. Pejler Structural requirements and mechanism for heparin-dependent activation and tetramerization of human beta I and beta II-tryptase J. Mol. Biol. 345 2005 129 139
    • (2005) J. Mol. Biol. , vol.345 , pp. 129-139
    • Hallgren, J.1    Lindahl, S.2    Pejler, G.3
  • 6
    • 0028881815 scopus 로고
    • The alpha form of human tryptase is the predominant type present in blood at baseline in normal subjects and is elevated in those with systemic mastocytosis
    • L.B. Schwartz, K. Sakai, T.R. Bradford, S.L. Ren, B. Zweiman, A.S. Worobec, and D.D. Metcalfe The alpha form of human tryptase is the predominant type present in blood at baseline in normal subjects and is elevated in those with systemic mastocytosis J. Clin. Invest. 96 1995 2702 2710
    • (1995) J. Clin. Invest. , vol.96 , pp. 2702-2710
    • Schwartz, L.B.1    Sakai, K.2    Bradford, T.R.3    Ren, S.L.4    Zweiman, B.5    Worobec, A.S.6    Metcalfe, D.D.7
  • 7
    • 0024434198 scopus 로고
    • Cloning and characterization of complementary-DNA for human tryptase
    • J.S. Miller, E.H. Westin, and L.B. Schwartz Cloning and characterization of complementary-DNA for human tryptase J. Clin. Invest. 84 1989 1188 1195
    • (1989) J. Clin. Invest. , vol.84 , pp. 1188-1195
    • Miller, J.S.1    Westin, E.H.2    Schwartz, L.B.3
  • 9
    • 0025053169 scopus 로고
    • Cloning and characterization of a second complementary DNA for human tryptase
    • J.S. Miller, G. Moxley, and L.B. Schwartz Cloning and characterization of a second complementary DNA for human tryptase J. Clin. Invest. 86 1990 864 870
    • (1990) J. Clin. Invest. , vol.86 , pp. 864-870
    • Miller, J.S.1    Moxley, G.2    Schwartz, L.B.3
  • 10
    • 0033525211 scopus 로고    scopus 로고
    • Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3
    • M. Pallaoro, M.S. Fejzo, L. Shayesteh, J.L. Blount, and G.H. Caughey Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3 J. Biol. Chem. 274 1999 3355 3362
    • (1999) J. Biol. Chem. , vol.274 , pp. 3355-3362
    • Pallaoro, M.1    Fejzo, M.S.2    Shayesteh, L.3    Blount, J.L.4    Caughey, G.H.5
  • 11
    • 0021044821 scopus 로고
    • Mammalian tissue trypsin-like enzymes-comparative reactivities of human-skin tryptase, human-lung tryptase, and bovine trypsin with peptide 4-nitroanilide and thioester substrates
    • T. Tanaka, B.J. Mcrae, K. Cho, R. Cook, J.E. Fraki, D.A. Johnson, and J.C. Powers Mammalian tissue trypsin-like enzymes-comparative reactivities of human-skin tryptase, human-lung tryptase, and bovine trypsin with peptide 4-nitroanilide and thioester substrates J. Biol. Chem. 258 1983 3552 3557
    • (1983) J. Biol. Chem. , vol.258 , pp. 3552-3557
    • Tanaka, T.1    McRae, B.J.2    Cho, K.3    Cook, R.4    Fraki, J.E.5    Johnson, D.A.6    Powers, J.C.7
  • 13
    • 0025455517 scopus 로고
    • Degradation of airway neuropeptides by human lung tryptase
    • E.K. Tam, and G.H. Caughey Degradation of airway neuropeptides by human lung tryptase Am. J. Respir. Cell Mol. Biol. 3 1990 27 32
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.3 , pp. 27-32
    • Tam, E.K.1    Caughey, G.H.2
  • 14
    • 0022388692 scopus 로고
    • The fibrinogenolytic activity of purified tryptase from human-lung mast-cells
    • L.B. Schwartz, T.R. Bradford, B.H. Littman, and B.U. Wintroub The fibrinogenolytic activity of purified tryptase from human-lung mast-cells J. Immunol. 135 1985 2762 2767
    • (1985) J. Immunol. , vol.135 , pp. 2762-2767
    • Schwartz, L.B.1    Bradford, T.R.2    Littman, B.H.3    Wintroub, B.U.4
  • 15
    • 0031467076 scopus 로고    scopus 로고
    • The tryptase, mouse mast cell protease 7, exhibits anticoagulant activity in vivo and in vitro due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma
    • C.F. Huang, G.W. Wong, N. Ghildyal, M.F. Gurish, A. Sali, and R. Matsumoto The tryptase, mouse mast cell protease 7, exhibits anticoagulant activity in vivo and in vitro due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma J. Biol. Chem. 272 1997 31885 31893
    • (1997) J. Biol. Chem. , vol.272 , pp. 31885-31893
    • Huang, C.F.1    Wong, G.W.2    Ghildyal, N.3    Gurish, M.F.4    Sali, A.5    Matsumoto, R.6
  • 16
    • 0031255314 scopus 로고    scopus 로고
    • Human tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12
    • S. Ren, A.E. Lawson, M. Carr, C.M. Baumgarten, and L.B. Schwartz Human tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12 J. Immunol. 159 1997 3540 3548
    • (1997) J. Immunol. , vol.159 , pp. 3540-3548
    • Ren, S.1    Lawson, A.E.2    Carr, M.3    Baumgarten, C.M.4    Schwartz, L.B.5
  • 17
    • 0032562226 scopus 로고    scopus 로고
    • Human mast cell tryptase fibrinogenolysis: Kinetics, anticoagulation mechanism, and cell adhesion disruption
    • V.A. Thomas, C.J. Wheeless, M.S. Stack, and D.A. Johnson Human mast cell tryptase fibrinogenolysis: kinetics, anticoagulation mechanism, and cell adhesion disruption Biochemistry 37 1998 2291 2298
    • (1998) Biochemistry , vol.37 , pp. 2291-2298
    • Thomas, V.A.1    Wheeless, C.J.2    Stack, M.S.3    Johnson, D.A.4
  • 18
    • 0037330931 scopus 로고    scopus 로고
    • Formation of active monomers from tetrameric human beta-tryptase
    • I. Fajardo, and G. Pejler Formation of active monomers from tetrameric human beta-tryptase Biochem. J. 369 2003 603 610
    • (2003) Biochem. J. , vol.369 , pp. 603-610
    • Fajardo, I.1    Pejler, G.2
  • 19
    • 0022872843 scopus 로고
    • Regulation of tryptase from human-lung mast-cells by heparin- stabilization of the active tetramer
    • L.B. Schwartz, and T.R. Bradford Regulation of tryptase from human-lung mast-cells by heparin-stabilization of the active tetramer J. Biol. Chem. 261 1986 7372 7379
    • (1986) J. Biol. Chem. , vol.261 , pp. 7372-7379
    • Schwartz, L.B.1    Bradford, T.R.2
  • 20
    • 0021148042 scopus 로고
    • Human-lung tryptase-purification and characterization
    • T.J. Smith, M.W. Hougland, and D.A. Johnson Human-lung tryptase-purification and characterization J. Biol. Chem. 259 1984 1046 1051
    • (1984) J. Biol. Chem. , vol.259 , pp. 1046-1051
    • Smith, T.J.1    Hougland, M.W.2    Johnson, D.A.3
  • 21
    • 0023680996 scopus 로고
    • Human-skin tryptase-purification, partial characterization and comparison with human-lung tryptase
    • I.T. Harvima, N.M. Schechter, R.J. Harvima, and J.E. Fraki Human-skin tryptase-purification, partial characterization and comparison with human-lung tryptase Biochim. Biophys. Acta 957 1988 71 80
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 71-80
    • Harvima, I.T.1    Schechter, N.M.2    Harvima, R.J.3    Fraki, J.E.4
  • 22
    • 14644415912 scopus 로고    scopus 로고
    • The interaction of human tryptase-beta with small molecule inhibitors provides new insights into the unusual functional instability and quaternary structure of the protease
    • T. Selwood, H. Smolensky, D.R. McCaslin, and N.M. Schechter The interaction of human tryptase-beta with small molecule inhibitors provides new insights into the unusual functional instability and quaternary structure of the protease Biochemistry 44 2005 3580 3590
    • (2005) Biochemistry , vol.44 , pp. 3580-3590
    • Selwood, T.1    Smolensky, H.2    McCaslin, D.R.3    Schechter, N.M.4
  • 23
    • 0025162150 scopus 로고
    • Interactions of human mast-cell tryptase with biological protease inhibitors
    • S.C. Alter, J.A. Kramps, A. Janoff, and L.B. Schwartz Interactions of human mast-cell tryptase with biological protease inhibitors Arch. Biochem. Biophys. 276 1990 26 31
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 26-31
    • Alter, S.C.1    Kramps, J.A.2    Janoff, A.3    Schwartz, L.B.4
  • 24
    • 0027469817 scopus 로고
    • Human skin tryptase-kinetic characterization of its spontaneous inactivation
    • N.M. Schechter, G.Y. Eng, and D.R. Mccaslin Human skin tryptase-kinetic characterization of its spontaneous inactivation Biochemistry 32 1993 2617 2625
    • (1993) Biochemistry , vol.32 , pp. 2617-2625
    • Schechter, N.M.1    Eng, G.Y.2    McCaslin, D.R.3
  • 25
    • 0029974125 scopus 로고    scopus 로고
    • Inactivation of human lung tryptase: Evidence for a re-activatable tetrameric intermediate and active monomers
    • A.K. Addington, and D.A. Johnson Inactivation of human lung tryptase: evidence for a re-activatable tetrameric intermediate and active monomers Biochemistry 35 1996 13511 13518
    • (1996) Biochemistry , vol.35 , pp. 13511-13518
    • Addington, A.K.1    Johnson, D.A.2
  • 26
    • 0029149499 scopus 로고
    • Structural changes associated with the spontaneous inactivation of the serine proteinase human tryptase
    • N.M. Schechter, G.Y. Eng, T. Selwood, and D.R. McCaslin Structural changes associated with the spontaneous inactivation of the serine proteinase human tryptase Biochemistry 34 1995 10628 10638
    • (1995) Biochemistry , vol.34 , pp. 10628-10638
    • Schechter, N.M.1    Eng, G.Y.2    Selwood, T.3    McCaslin, D.R.4
  • 27
    • 0032080451 scopus 로고    scopus 로고
    • Regulation of human mast cell beta-tryptase: Conversion of inactive monomer to active tetramer at acid pH
    • S.L. Ren, K. Sakai, and L.B. Schwartz Regulation of human mast cell beta-tryptase: conversion of inactive monomer to active tetramer at acid pH J. Immunol. 160 1998 4561 4569
    • (1998) J. Immunol. , vol.160 , pp. 4561-4569
    • Ren, S.L.1    Sakai, K.2    Schwartz, L.B.3
  • 28
    • 2642600031 scopus 로고    scopus 로고
    • Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
    • P.J. Pereira, A. Bergner, S. Macedo-Ribeiro, R. Huber, G. Matschiner, and H. Fritz Human beta-tryptase is a ring-like tetramer with active sites facing a central pore Nature 392 1998 306 311
    • (1998) Nature , vol.392 , pp. 306-311
    • Pereira, P.J.1    Bergner, A.2    MacEdo-Ribeiro, S.3    Huber, R.4    Matschiner, G.5    Fritz, H.6
  • 29
    • 0035860703 scopus 로고    scopus 로고
    • Definition of the extended substrate specificity determinants for beta-tryptases I and II
    • J.L. Harris, A. Niles, K. Burdick, M. Maffitt, B.J. Backes, and J.A. Ellman Definition of the extended substrate specificity determinants for beta-tryptases I and II J. Biol. Chem. 276 2001 34941 34947
    • (2001) J. Biol. Chem. , vol.276 , pp. 34941-34947
    • Harris, J.L.1    Niles, A.2    Burdick, K.3    Maffitt, M.4    Backes, B.J.5    Ellman, J.A.6
  • 30
    • 0033538454 scopus 로고    scopus 로고
    • Human tryptases alpha and beta/II are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft
    • C. Huang, L. Li, S.A. Krilis, K. Chanasyk, Y. Tang, and Z. Li Human tryptases alpha and beta/II are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft J. Biol. Chem. 274 1999 19670 19676
    • (1999) J. Biol. Chem. , vol.274 , pp. 19670-19676
    • Huang, C.1    Li, L.2    Krilis, S.A.3    Chanasyk, K.4    Tang, Y.5    Li, Z.6
  • 31
    • 0037066138 scopus 로고    scopus 로고
    • Diverse stability and catalytic properties of human tryptase alpha and beta isoforms are mediated by residue differences at the S1 pocket
    • T. Selwood, Z.M. Wang, D.R. McCaslin, and N.M. Schechter Diverse stability and catalytic properties of human tryptase alpha and beta isoforms are mediated by residue differences at the S1 pocket Biochemistry 41 2002 3329 3340
    • (2002) Biochemistry , vol.41 , pp. 3329-3340
    • Selwood, T.1    Wang, Z.M.2    McCaslin, D.R.3    Schechter, N.M.4
  • 32
    • 0036385841 scopus 로고    scopus 로고
    • The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region
    • U. Marquardt, F. Zettl, R. Huber, W. Bode, and C. Sommerhoff The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region J. Mol. Biol. 321 2002 491 502
    • (2002) J. Mol. Biol. , vol.321 , pp. 491-502
    • Marquardt, U.1    Zettl, F.2    Huber, R.3    Bode, W.4    Sommerhoff, C.5
  • 33
    • 0026534774 scopus 로고
    • Alpha 1-6(alpha 1-3)-difucosylation of the asparagine-bound N-acetylglucosamine in honeybee venom phospholipase A2
    • E. Staudacher, F. Altmann, L. Marz, K. Hard, J.P. Kamerling, and J.F. Vliegenthart Alpha 1-6(alpha 1-3)-difucosylation of the asparagine-bound N-acetylglucosamine in honeybee venom phospholipase A2 Glycoconj. J. 9 1992 82 85
    • (1992) Glycoconj. J. , vol.9 , pp. 82-85
    • Staudacher, E.1    Altmann, F.2    Marz, L.3    Hard, K.4    Kamerling, J.P.5    Vliegenthart, J.F.6
  • 34
    • 0029852531 scopus 로고    scopus 로고
    • Haemonchus contortus glycoproteins contain N-linked oligosaccharides with novel highly fucosylated core structures
    • S.M. Haslam, G.C. Coles, E.A. Munn, T.S. Smith, H.F. Smith, H.R. Morris, and A. Dell Haemonchus contortus glycoproteins contain N-linked oligosaccharides with novel highly fucosylated core structures J. Biol. Chem. 271 1996 30561 30570
    • (1996) J. Biol. Chem. , vol.271 , pp. 30561-30570
    • Haslam, S.M.1    Coles, G.C.2    Munn, E.A.3    Smith, T.S.4    Smith, H.F.5    Morris, H.R.6    Dell, A.7
  • 35
    • 0037244415 scopus 로고    scopus 로고
    • The heterogeneity of mast cell tryptase from human lung and skin-differences in size, charge and substrate affinity
    • Q. Peng, A.R. McEuen, R.C. Benyon, and A.F. Walls The heterogeneity of mast cell tryptase from human lung and skin-differences in size, charge and substrate affinity Eur. J. Biochem. 270 2003 270 283
    • (2003) Eur. J. Biochem. , vol.270 , pp. 270-283
    • Peng, Q.1    McEuen, A.R.2    Benyon, R.C.3    Walls, A.F.4
  • 36
    • 33947092515 scopus 로고
    • Structural basis of activation and action of trypsin
    • R. Huber, and W. Bode Structural basis of activation and action of trypsin Accts Chem. Res. 11 1978 114 122
    • (1978) Accts Chem. Res. , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 37
    • 0022273818 scopus 로고
    • The 1.8 Å structure of the complex between chymostatin and Streptomyces griseus protease-A: A model for serine protease catalytic tetrahedral intermediates
    • L.T.J. Delbaere, and G.D. Brayer The 1.8 Å structure of the complex between chymostatin and Streptomyces griseus protease-A: a model for serine protease catalytic tetrahedral intermediates J. Mol. Biol. 183 1985 89 103
    • (1985) J. Mol. Biol. , vol.183 , pp. 89-103
    • Delbaere, L.T.J.1    Brayer, G.D.2
  • 38
    • 0032518496 scopus 로고    scopus 로고
    • Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: Location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
    • G. Guncar, M. Podobnik, J. Pungercar, B. Strukelj, V. Turk, and D. Turk Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function Structure 6 1998 51 61
    • (1998) Structure , vol.6 , pp. 51-61
    • Guncar, G.1    Podobnik, M.2    Pungercar, J.3    Strukelj, B.4    Turk, V.5    Turk, D.6
  • 40
    • 0025923430 scopus 로고
    • Glu-192→Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin
    • B.F. Le Bonniec, and C.T. Esmon Glu-192→Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin Proc. Natl Acad. Sci. USA 88 1991 7371 7375
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7371-7375
    • Le Bonniec, B.F.1    Esmon, C.T.2
  • 41
    • 0029118088 scopus 로고
    • Identification of thrombin residues that modulate its interactions with antithrombin-III and alpha-1-antitrypsin
    • B.F. Le Bonniec, E.R. Guinto, and S.R. Stone Identification of thrombin residues that modulate its interactions with antithrombin-III and alpha-1-antitrypsin Biochemistry 34 1995 12241 12248
    • (1995) Biochemistry , vol.34 , pp. 12241-12248
    • Le Bonniec, B.F.1    Guinto, E.R.2    Stone, S.R.3
  • 42
    • 0028174260 scopus 로고
    • Glu192→Gln substitution in thrombin yields an enzyme that is effectively inhibited by bovine pancreatic trypsin inhibitor and tissue factor pathway inhibitor
    • E.R. Guinto, J. Ye, B.F. Le Bonniec, and C.T. Esmon Glu192→Gln substitution in thrombin yields an enzyme that is effectively inhibited by bovine pancreatic trypsin inhibitor and tissue factor pathway inhibitor J. Biol. Chem. 269 1994 18395 18400
    • (1994) J. Biol. Chem. , vol.269 , pp. 18395-18400
    • Guinto, E.R.1    Ye, J.2    Le Bonniec, B.F.3    Esmon, C.T.4
  • 43
    • 0030959346 scopus 로고    scopus 로고
    • The thrombin E192Q-BPTI complex reveals gross structural rearrangements: Implications for the interaction with antithrombin and thrombomodulin
    • A. van de Locht, W. Bode, R. Huber, B.F. Le Bonniec, S.R. Stone, C.T. Esmon, and M.T. Stubbs The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin EMBO J. 16 1997 2977 2984
    • (1997) EMBO J. , vol.16 , pp. 2977-2984
    • Van De Locht, A.1    Bode, W.2    Huber, R.3    Le Bonniec, B.F.4    Stone, S.R.5    Esmon, C.T.6    Stubbs, M.T.7
  • 46
    • 0842304458 scopus 로고    scopus 로고
    • Inhibitors of serine proteases as potential therapeutic agents: The road from thrombin to tryptase to cathepsin G
    • B.E. Maryanoff Inhibitors of serine proteases as potential therapeutic agents: the road from thrombin to tryptase to cathepsin G J. Med. Chem. 47 2004 769 787
    • (2004) J. Med. Chem. , vol.47 , pp. 769-787
    • Maryanoff, B.E.1
  • 47
    • 0037083293 scopus 로고    scopus 로고
    • Tryptase inhibition blocks airway inflammation in a mouse asthma model
    • S.W. Oh, C.I. Pae, D.K. Lee, F. Jones, G.K.S. Chiang, and H.O. Kim Tryptase inhibition blocks airway inflammation in a mouse asthma model J. Immunol. 168 2002 1992 2000
    • (2002) J. Immunol. , vol.168 , pp. 1992-2000
    • Oh, S.W.1    Pae, C.I.2    Lee, D.K.3    Jones, F.4    Chiang, G.K.S.5    Kim, H.O.6
  • 48
    • 10644257614 scopus 로고    scopus 로고
    • Inhibitors of mast cell tryptase beta as therapeutics for the treatment of asthma and inflammatory disorders
    • J.A. Cairns Inhibitors of mast cell tryptase beta as therapeutics for the treatment of asthma and inflammatory disorders Pulmon. Pharmacol. Therapeut. 18 2005 55 66
    • (2005) Pulmon. Pharmacol. Therapeut. , vol.18 , pp. 55-66
    • Cairns, J.A.1
  • 50
    • 0017107996 scopus 로고
    • Induction of bovine trypsinogen-trypsin transition by peptides sequentially similar to N-terminus of trypsin
    • W. Bode, and R. Huber Induction of bovine trypsinogen-trypsin transition by peptides sequentially similar to N-terminus of trypsin FEBS Letters 68 1976 231 236
    • (1976) FEBS Letters , vol.68 , pp. 231-236
    • Bode, W.1    Huber, R.2
  • 51
    • 0141929350 scopus 로고    scopus 로고
    • Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation
    • R. Friedrich, P. Panizzi, P. Fuentes-Prior, K. Richter, I. Verhamme, and P.J. Anderson Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation Nature 425 2003 535 539
    • (2003) Nature , vol.425 , pp. 535-539
    • Friedrich, R.1    Panizzi, P.2    Fuentes-Prior, P.3    Richter, K.4    Verhamme, I.5    Anderson, P.J.6
  • 52
    • 0028801352 scopus 로고
    • X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B
    • H. Brandstetter, M. Bauer, R. Huber, P. Lollar, and W. Bode X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B Proc. Natl Acad. Sci. USA 92 1995 9796 9800
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9796-9800
    • Brandstetter, H.1    Bauer, M.2    Huber, R.3    Lollar, P.4    Bode, W.5
  • 53
    • 0037423301 scopus 로고    scopus 로고
    • Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop
    • K. Sichler, E. Kopetzki, R. Huber, W. Bode, K.P. Hopfner, and H. Brandstetter Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop J. Biol. Chem. 278 2003 4121 4126
    • (2003) J. Biol. Chem. , vol.278 , pp. 4121-4126
    • Sichler, K.1    Kopetzki, E.2    Huber, R.3    Bode, W.4    Hopfner, K.P.5    Brandstetter, H.6
  • 54
    • 0037007616 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine (vol 416, pg 455, 2002)
    • T. Krojer, M. Garrido-Franco, R. Huber, M. Ehrmann, and T. Clausen Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine (vol 416, pg 455, 2002) Nature 417 2002 102
    • (2002) Nature , vol.417 , pp. 102
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 55
    • 0032500627 scopus 로고    scopus 로고
    • Structures of native and complexed complement factor D: Implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity
    • H. Jing, Y.S. Babu, D. Moore, J.M. Kilpatrick, X.Y. Liu, J.E. Volanakis, and S.V. Narayana Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity J. Mol. Biol. 282 1998 1061 1081
    • (1998) J. Mol. Biol. , vol.282 , pp. 1061-1081
    • Jing, H.1    Babu, Y.S.2    Moore, D.3    Kilpatrick, J.M.4    Liu, X.Y.5    Volanakis, J.E.6    Narayana, S.V.7
  • 56
    • 1842816463 scopus 로고    scopus 로고
    • Structural analysis of engineered Bb fragment of complement factor B: Insights into the activation mechanism of the alternative pathway C3-convertase
    • K. Ponnuraj, Y. Xu, K. Macon, D. Moore, J.E. Volanakis, and S.V. Narayana Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase Mol. Cell 14 2004 17 28
    • (2004) Mol. Cell , vol.14 , pp. 17-28
    • Ponnuraj, K.1    Xu, Y.2    MacOn, K.3    Moore, D.4    Volanakis, J.E.5    Narayana, S.V.6
  • 57
    • 0037184613 scopus 로고    scopus 로고
    • The 2.2-Å crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual features
    • C. Hink-Schauer, E. Estebanez-Perpina, E. Wilharm, P. Fuentes-Prior, and W. Klinkert The 2.2-Å crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual features J. Biol. Chem. 277 2002 50923 50933
    • (2002) J. Biol. Chem. , vol.277 , pp. 50923-50933
    • Hink-Schauer, C.1    Estebanez-Perpina, E.2    Wilharm, E.3    Fuentes-Prior, P.4    Klinkert, W.5
  • 58
    • 13844296946 scopus 로고    scopus 로고
    • Conformational lability in serine protease active sites: Structures of hepatocyte growth factor activator (HGFA) alone and with the inhibitory domain from HGFA inhibitor-1B
    • S. Shia, J. Stamos, D. Kirchhofer, B. Fan, J. Wu, and R.T. Corpuz Conformational lability in serine protease active sites: structures of hepatocyte growth factor activator (HGFA) alone and with the inhibitory domain from HGFA inhibitor-1B J. Mol. Biol. 346 2005 1335 1349
    • (2005) J. Mol. Biol. , vol.346 , pp. 1335-1349
    • Shia, S.1    Stamos, J.2    Kirchhofer, D.3    Fan, B.4    Wu, J.5    Corpuz, R.T.6
  • 59
    • 0036382902 scopus 로고    scopus 로고
    • Crystal structure of a prostate kallikrein isolated from stallion seminal plasma: A homologue of human PSA
    • A.L. Carvalho, L. Sanz, D. Barettino, A. Romero, J.J. Calvete, and M.J. Romao Crystal structure of a prostate kallikrein isolated from stallion seminal plasma: a homologue of human PSA J. Mol. Biol. 322 2002 325 337
    • (2002) J. Mol. Biol. , vol.322 , pp. 325-337
    • Carvalho, A.L.1    Sanz, L.2    Barettino, D.3    Romero, A.4    Calvete, J.J.5    Romao, M.J.6
  • 61
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • J.J. Perona, and C.S. Craik Structural basis of substrate specificity in the serine proteases Protein Sci. 4 1995 337 360
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 64
    • 84920325457 scopus 로고
    • AMoRe-an automated package for molecular replacement
    • J. Navaza AMoRe-an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 66
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • R.A. Engh, and R. Huber Accurate bond and angle parameters for X-ray protein-structure refinement Acta Crystallog. sect. A 47 1991 392 400
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 69
    • 0000023777 scopus 로고
    • The CCP4 suite: Programs for cystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 The CCP4 suite: programs for cystallography Acta Crystallog. sect. D 50 1994 157 163
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 157-163
  • 71
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 72
    • 0027968068 scopus 로고
    • CLUSTAL W.: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W.: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 22 1994 4673 4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 73
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • G.J. Barton ALSCRIPT: a tool to format multiple sequence alignments Protein Eng. 6 1993 37 40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 74
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 75
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Struct. Funct. Genet. 11 1991 281 296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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