메뉴 건너뛰기




Volumn 42, Issue 21, 2003, Pages 6484-6492

The role of the protein core in the inhibitory power of the classic serine protease inhibitor, chymotrypsin inhibitor 2

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CRYSTAL STRUCTURE; ENZYME INHIBITION; HYDROLYSIS; MUTAGENESIS; SUBSTRATES;

EID: 0037672714     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034275d     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode, W., and Huber, R. (1992) Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204, 433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 2
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M., Jr., and Kato, I. (1980) Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski M., Jr.1    Kato, I.2
  • 3
    • 0001289399 scopus 로고
    • Amino acid sequence homology between a serine protease inhibitor from barley and potato I inhibitor
    • Svendsen, I., Jonassen, I., Hejgaard, J., and Boisen, S. (1980) Amino acid sequence homology between a serine protease inhibitor from barley and potato I inhibitor. Carlsberg Res. Commun. 45, 389-395.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 389-395
    • Svendsen, I.1    Jonassen, I.2    Hejgaard, J.3    Boisen, S.4
  • 4
    • 85024813985 scopus 로고
    • Inhibitors of chymotrypsin and microbial serine proteases in barley grains
    • Boisen, S., Andersen, C. Y., and Hejgaard, J. (1981) Inhibitors of chymotrypsin and microbial serine proteases in barley grains. Physiol. Plant. 52, 167-176.
    • (1981) Physiol. Plant. , vol.52 , pp. 167-176
    • Boisen, S.1    Andersen, C.Y.2    Hejgaard, J.3
  • 5
    • 0000818624 scopus 로고
    • Crystal and molecular structure of chymotrypsin inhibitor 2 from barley seeds in complex with subtilisin Novo
    • McPhalen, C. A., Svendsen, I., Jonassen, I., and James, M. N. G. (1985) Crystal and molecular structure of chymotrypsin inhibitor 2 from barley seeds in complex with subtilisin Novo. Proc. Natl. Acad. Sci. U.S.A. 82, 7242-7246.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 7242-7246
    • McPhalen, C.A.1    Svendsen, I.2    Jonassen, I.3    James, M.N.G.4
  • 6
    • 0036678453 scopus 로고    scopus 로고
    • A clogged gutter mechanism for protease inhibitors
    • Radisky, E. S., and Koshland, D. E., Jr. (2002) A clogged gutter mechanism for protease inhibitors. Proc. Natl. Acad. Sci. U.S.A. 99, 10316-10321.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10316-10321
    • Radisky, E.S.1    Koshland D.E., Jr.2
  • 7
    • 0026314941 scopus 로고
    • Design of a small peptide-based proteinase inhibitor by modeling the active site region of barley chymotrypsin inhibitor 2
    • Leatherbarrow, R. J., and Salacinski, H. J. (1991) Design of a small peptide-based proteinase inhibitor by modeling the active site region of barley chymotrypsin inhibitor 2. Biochemistry 30, 10717-10721.
    • (1991) Biochemistry , vol.30 , pp. 10717-10721
    • Leatherbarrow, R.J.1    Salacinski, H.J.2
  • 8
    • 0021112782 scopus 로고
    • Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis
    • Wells, J. A., Ferrari, E., Henner, D. J., Estell, D. A., and Chen, E. Y. (1983) Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis. Nucleic Acids Res. 11, 7911-7925.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 7911-7925
    • Wells, J.A.1    Ferrari, E.2    Henner, D.J.3    Estell, D.A.4    Chen, E.Y.5
  • 9
    • 0021228872 scopus 로고
    • Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation
    • Yang, M. Y., Ferrari, E., and Henner, D. J. (1984) Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation, J. Bacteriol. 160, 15-21.
    • (1984) J. Bacteriol. , vol.160 , pp. 15-21
    • Yang, M.Y.1    Ferrari, E.2    Henner, D.J.3
  • 10
    • 0014124267 scopus 로고
    • Development of competence in the Bacillus subtilis transformation system
    • Bott, K. F., and Wilson, G. A. (1967) Development of competence in the Bacillus subtilis transformation system. J. Bacteriol. 94, 562-570.
    • (1967) J. Bacteriol. , vol.94 , pp. 562-570
    • Bott, K.F.1    Wilson, G.A.2
  • 11
    • 0014272140 scopus 로고
    • Nutritional factors influencing the development of competence in the Bacillus subtilis transformation system
    • Wilson, G. A., and Bott, K. F. (1968) Nutritional factors influencing the development of competence in the Bacillus subtilis transformation system. J. Bacteriol. 95, 1439-1449.
    • (1968) J. Bacteriol. , vol.95 , pp. 1439-1449
    • Wilson, G.A.1    Bott, K.F.2
  • 12
    • 73049152989 scopus 로고
    • The spectrophotometric determination of the operational normality of an α-chymotrypsin solution
    • Schonbaum, G. R., Zerner, B., and Bender, M. L. (1961) The spectrophotometric determination of the operational normality of an α-chymotrypsin solution. J. Biol. Chem. 236, 2930-2935.
    • (1961) J. Biol. Chem. , vol.236 , pp. 2930-2935
    • Schonbaum, G.R.1    Zerner, B.2    Bender, M.L.3
  • 15
    • 77956939074 scopus 로고
    • Protein proteinase inhibitors - Molecular aspects
    • Laskowski, M., Jr., and Sealock, R. W. (1971) Protein Proteinase Inhibitors - Molecular Aspects. The Enzymes 3rd ed., Vol. 3, pp 375-473.
    • (1971) The Enzymes 3rd Ed. , vol.3 , pp. 375-473
    • Laskowski M., Jr.1    Sealock, R.W.2
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0025369318 scopus 로고
    • Recombinant chymotrypsin inhibitor 2: Expression, kinetic analysis of inhibition with α-chymotrypsin and wild-type and mutant subtilisin BPN', and protein engineering to investigate inhibitory specificity and mechanism
    • Longstaff, C., Campbell, A. F., and Fersht, A. R. (1990) Recombinant chymotrypsin inhibitor 2: expression, kinetic analysis of inhibition with α-chymotrypsin and wild-type and mutant subtilisin BPN', and protein engineering to investigate inhibitory specificity and mechanism. Biochemistry 29, 7339-7347.
    • (1990) Biochemistry , vol.29 , pp. 7339-7347
    • Longstaff, C.1    Campbell, A.F.2    Fersht, A.R.3
  • 18
    • 0036808537 scopus 로고    scopus 로고
    • FindPept, a tool to identify unmatched masses in peptide mass fingerprinting protein identification
    • Gattiker, A., Bienvenut, W. V., Bairoch, A., and Gasteiger E. (2002) FindPept, a tool to identify unmatched masses in peptide mass fingerprinting protein identification. Proteomics 2, 1435-1444.
    • (2002) Proteomics , vol.2 , pp. 1435-1444
    • Gattiker, A.1    Bienvenut, W.V.2    Bairoch, A.3    Gasteiger, E.4
  • 21
    • 0027959459 scopus 로고
    • Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity
    • Jackson, S. E., and Fersht, A. R. (1994) Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity. Biochemistry 33, 13880-13887.
    • (1994) Biochemistry , vol.33 , pp. 13880-13887
    • Jackson, S.E.1    Fersht, A.R.2
  • 22
    • 0033912828 scopus 로고    scopus 로고
    • A novel artificial loop scaffold for the noncovalent constraint of peptides
    • Gururaja, T. L., Narasimhamurthy, S., Payan, D. G., and Anderson, D. C. (2000) A novel artificial loop scaffold for the noncovalent constraint of peptides. Chem. Biol. 7, 515-527.
    • (2000) Chem. Biol. , vol.7 , pp. 515-527
    • Gururaja, T.L.1    Narasimhamurthy, S.2    Payan, D.G.3    Anderson, D.C.4
  • 23
    • 0020688134 scopus 로고
    • Kinetics of subtilisin and thiolsubtilisin
    • Philipp, M., and Bender, M. L. (1983) Kinetics of subtilisin and thiolsubtilisin. Mol. Cell. Biochem. 51, 5-32.
    • (1983) Mol. Cell. Biochem. , vol.51 , pp. 5-32
    • Philipp, M.1    Bender, M.L.2
  • 24
    • 0016333650 scopus 로고
    • Comparative study of various serine alkaline proteinases from microorganisms
    • Morihara, K., Oka, T., and Tsuzuki, H. (1974) Comparative study of various serine alkaline proteinases from microorganisms. Arch. Biochem. Biophys. 165, 72-79.
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 72-79
    • Morihara, K.1    Oka, T.2    Tsuzuki, H.3
  • 25
  • 26
    • 0000453071 scopus 로고
    • Importance of hydrogen-bond formation in stabilizing the transition state of subtilisin
    • Wells, J. A., Cunningham, B. C., Graycar, T. P., and Estell, D. A. (1986) Importance of hydrogen-bond formation in stabilizing the transition state of subtilisin. Philos. Trans. R. Soc. London A 317, 415-423.
    • (1986) Philos. Trans. R. Soc. London A , vol.317 , pp. 415-423
    • Wells, J.A.1    Cunningham, B.C.2    Graycar, T.P.3    Estell, D.A.4
  • 28
    • 0033485402 scopus 로고    scopus 로고
    • Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library
    • McBride, J. D., Freeman, H. N. M., and Leatherbarrow, R. J. (1999) Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library. Eur. J. Biochem. 266, 403-412.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 403-412
    • McBride, J.D.1    Freeman, H.N.M.2    Leatherbarrow, R.J.3
  • 30
    • 0035793719 scopus 로고    scopus 로고
    • The Bowman-Birk inhibitor reactive site loop sequence represents an independent structural β-hairpin motif
    • Brauer, A. B. E., Kelly, G., McBride, J. D., Cooke, R. M., Matthews, S. J., and Leatherbarrow, R. J. (2001) The Bowman-Birk inhibitor reactive site loop sequence represents an independent structural β-hairpin motif. J. Mol. Biol. 306, 799-807.
    • (2001) J. Mol. Biol. , vol.306 , pp. 799-807
    • Brauer, A.B.E.1    Kelly, G.2    McBride, J.D.3    Cooke, R.M.4    Matthews, S.J.5    Leatherbarrow, R.J.6
  • 31
    • 0032981632 scopus 로고    scopus 로고
    • Comparison of protein-protein interactions in serine protease-inhibitor and antibody-antigen complexes: Implications for the protein docking problem
    • Jackson, R. M. (1999) Comparison of protein-protein interactions in serine protease-inhibitor and antibody-antigen complexes: Implications for the protein docking problem. Protein Sci. 8, 603-613.
    • (1999) Protein Sci. , vol.8 , pp. 603-613
    • Jackson, R.M.1
  • 32
    • 0025912338 scopus 로고
    • Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors
    • Hubbard, S. J., Campbell, S. F., and Thornton, J. M. (1991) Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors. J. Mol. Biol. 220, 507-530.
    • (1991) J. Mol. Biol. , vol.220 , pp. 507-530
    • Hubbard, S.J.1    Campbell, S.F.2    Thornton, J.M.3
  • 33
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona, J. J., and Craik, C. S. (1995) Structural basis of substrate specificity in the serine proteases. Protein Sci. 4, 337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 36
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?
    • Laskowski, M., Jr., and Qasim, M. A. (2000) What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes? Biochim. Biophys. Acta 1477, 324-337.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 324-337
    • Laskowski M., Jr.1    Qasim, M.A.2
  • 37
    • 0022445901 scopus 로고
    • Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering
    • Estell, D. A., Graycar, T. P., Miller, J. V., Powers, D. B., Burnier, J. P., Ng, P. G., and Wells, J. A. (1986) Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering. Science 233, 659-663.
    • (1986) Science , vol.233 , pp. 659-663
    • Estell, D.A.1    Graycar, T.P.2    Miller, J.V.3    Powers, D.B.4    Burnier, J.P.5    Ng, P.G.6    Wells, J.A.7
  • 38
    • 0023394374 scopus 로고
    • Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering
    • Wells, J. A., Cunningham, B. C., Graycar, T. P., and Estell, D. A. (1987) Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering. Proc. Natl. Acad. Sci. U.S.A. 84, 5167-5171.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5167-5171
    • Wells, J.A.1    Cunningham, B.C.2    Graycar, T.P.3    Estell, D.A.4
  • 39
    • 0034603736 scopus 로고    scopus 로고
    • Deciphering the role of the electrostatic interactions involving Gly70 in eglin c by total chemical protein synthesis
    • Lu, W.-Y., Starovasnik, M. A., Dwyer, J. J., Kossiakoff, A. A., Kent, S. B. H., and Lu, W. (2000) Deciphering the role of the electrostatic interactions involving Gly70 in eglin c by total chemical protein synthesis. Biochemistry 39, 3575-3584.
    • (2000) Biochemistry , vol.39 , pp. 3575-3584
    • Lu, W.-Y.1    Starovasnik, M.A.2    Dwyer, J.J.3    Kossiakoff, A.A.4    Kent, S.B.H.5    Lu, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.