메뉴 건너뛰기




Volumn 290, Issue 2, 1999, Pages 525-533

High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds

Author keywords

Bowman Birk inhibitor; Cyclic peptide; Sunflower seeds; Trypsin inhibitor; X ray crystallography

Indexed keywords

BOWMAN BIRK INHIBITOR; CYCLOPEPTIDE; SERINE PROTEINASE INHIBITOR; TRYPSIN;

EID: 0344655676     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2891     Document Type: Article
Times cited : (339)

References (30)
  • 1
    • 0024791521 scopus 로고
    • Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density
    • Bartunik H. D., Summers L. J., Bartsch H. H. Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density. J. Mol. Biol. 210:1989;813-828.
    • (1989) J. Mol. Biol. , vol.210 , pp. 813-828
    • Bartunik, H.D.1    Summers, L.J.2    Bartsch, H.H.3
  • 2
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interactions with proteinase
    • Bode W., Huber R. Natural protein proteinase inhibitors and their interactions with proteinase. Eur. J. Biochem. 204:1992;433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 5
    • 0029034507 scopus 로고
    • Synthesis of a mixture of cyclic-peptides based on the Bowman-Birk reactive-site loop to screen for serine-protease inhibitors
    • Domingo G. J., Leatherbarrow R. J., Freeman N., Patel S., Weir M. Synthesis of a mixture of cyclic-peptides based on the Bowman-Birk reactive-site loop to screen for serine-protease inhibitors. Int. J. Peptide Protein Res. 46:1995;79-87.
    • (1995) Int. J. Peptide Protein Res. , vol.46 , pp. 79-87
    • Domingo, G.J.1    Leatherbarrow, R.J.2    Freeman, N.3    Patel, S.4    Weir, M.5
  • 6
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger B. F., Kokowsky N., Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochim. Biophys. 95:1961;271-278.
    • (1961) Arch. Biochim. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 7
    • 0029985841 scopus 로고    scopus 로고
    • Comparison of the structures of the cyclotheonamide A complexes of human α-thrombin and bovine β-trypsin
    • Ganesh V., Lee A. Y., Clardy J., Tulinsky A. Comparison of the structures of the cyclotheonamide A complexes of human α-thrombin and bovine β-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
  • 8
    • 0030795530 scopus 로고    scopus 로고
    • Stability of protease inhibitors based on the Bowman-Birk reactive site loop to hydrolysis by proteases
    • Gariani T., Leatherbarrow R. J. Stability of protease inhibitors based on the Bowman-Birk reactive site loop to hydrolysis by proteases. J. Peptide Res. 49:1997;467-475.
    • (1997) J. Peptide Res. , vol.49 , pp. 467-475
    • Gariani, T.1    Leatherbarrow, R.J.2
  • 9
    • 0027516857 scopus 로고
    • Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family
    • Huang Q., Liu S., Tang Y. Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family. J. Mol. Biol. 229:1993;1022-1036.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1022-1036
    • Huang, Q.1    Liu, S.2    Tang, Y.3
  • 10
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 11
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49:1980;593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 12
  • 13
    • 0027953720 scopus 로고
    • Studies on an artificial trypsin inhibitor peptide derived from the Mung bean trypsin inhibitor: Chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin
    • Li Y., Huang Q., Zhang S., Liu S., Chi C., Tang Y. Studies on an artificial trypsin inhibitor peptide derived from the Mung bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin. J. Biochem. 116:1994;18-25.
    • (1994) J. Biochem. , vol.116 , pp. 18-25
    • Li, Y.1    Huang, Q.2    Zhang, S.3    Liu, S.4    Chi, C.5    Tang, Y.6
  • 14
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in trypsin, tryspsinogen and its complex with inhibitors
    • Marquart M., Walter J., Drisenhofer J., Bode W., Huber R. The geometry of the reactive site and of the peptide groups in trypsin, tryspsinogen and its complex with inhibitors. Acta Crystallog. sect. B. 39:1983;480-490.
    • (1983) Acta Crystallog. Sect. B , vol.39 , pp. 480-490
    • Marquart, M.1    Walter, J.2    Drisenhofer, J.3    Bode, W.4    Huber, R.5
  • 15
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G. N., Vagin A. A., 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
  • 16
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. 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
  • 17
    • 0017378998 scopus 로고
    • Studies on the synthesis of proteinase inhibitors
    • Nishino N., Aoyagi H., Kato T., Izumiya N. Studies on the synthesis of proteinase inhibitors. J. Biochem. 82:1977;901-909.
    • (1977) J. Biochem. , vol.82 , pp. 901-909
    • Nishino, N.1    Aoyagi, H.2    Kato, T.3    Izumiya, N.4
  • 18
    • 0015840847 scopus 로고
    • Studies on soybean trypsin inhibitors. VIII. Disulphide bridges in soybean Bowman-Birk proteinase inhibitors
    • Odani S., Ikenaka T. Studies on soybean trypsin inhibitors. VIII. Disulphide bridges in soybean Bowman-Birk proteinase inhibitors. J. Biochem. 74:1973;697-715.
    • (1973) J. Biochem. , vol.74 , pp. 697-715
    • Odani, S.1    Ikenaka, T.2
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., 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
  • 20
    • 0020475594 scopus 로고
    • Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model-building studies of comlexes serine
    • Papamokos E., Weber E., Bode W., Huber R., Empie M. W., Kato I., Lakowski M. Jr. Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model-building studies of comlexes serine. J. Mol. Biol. 158:1982;515-537.
    • (1982) J. Mol. Biol. , vol.158 , pp. 515-537
    • Papamokos, E.1    Weber, E.2    Bode, W.3    Huber, R.4    Empie, M.W.5    Kato, I.6    Lakowski M., Jr.7
  • 21
    • 0031557387 scopus 로고    scopus 로고
    • Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
    • Ranson N. A., Burston S. G., Clarke A. R. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J. Mol. Biol. 266:1997;656-664.
    • (1997) J. Mol. Biol. , vol.266 , pp. 656-664
    • Ranson, N.A.1    Burston, S.G.2    Clarke, A.R.3
  • 22
    • 0001144526 scopus 로고
    • Seed storage proteins: The enzymes inhibitors. Methods in Plant
    • Richardson M. Seed storage proteins: the enzymes inhibitors. Methods in Plant. Biochemistry. 5:1991;259-305.
    • (1991) Biochemistry , vol.5 , pp. 259-305
    • Richardson, M.1
  • 23
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defences against insects and pathogens
    • Ryan C. A. Protease inhibitors in plants: genes for improving defences against insects and pathogens. Annu. Rev. of Phytopath. 28:1990;425-449.
    • (1990) Annu. Rev. of Phytopath. , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 24
    • 0014211618 scopus 로고
    • On the size of the active site proteases. I. Papain
    • Schechter I., Berger A. On the size of the active site proteases. I. Papain. Biochim. Biophys. Res. Commun. 27:1967;157-162.
    • (1967) Biochim. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 25
    • 0000078132 scopus 로고    scopus 로고
    • Enzyme inhibitors of seeds: Types and properties
    • P. R. Shewry, & R. Casey. Dordrecht: Kluwer Academic Publishers
    • Shewry P. R. Enzyme inhibitors of seeds: types and properties. Shewry P. R., Casey R. Seed Proteins. 1999;Kluwer Academic Publishers, Dordrecht.
    • (1999) Seed Proteins
    • Shewry, P.R.1
  • 26
    • 77956761508 scopus 로고    scopus 로고
    • Plant proteins that confer resistance to pests and pathogens
    • Shewry P. R., Lucas J. A. Plant proteins that confer resistance to pests and pathogens. Advan. Botan. Res. 26:1997;135-192.
    • (1997) Advan. Botan. Res. , vol.26 , pp. 135-192
    • Shewry, P.R.1    Lucas, J.A.2
  • 29
    • 0029658121 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution
    • Voss R., Ermler U., Essen L., Wenzl G., Kim Y., Flecker P. Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Eur. J. Biochem. 242:1996;122-131.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 122-131
    • Voss, R.1    Ermler, U.2    Essen, L.3    Wenzl, G.4    Kim, Y.5    Flecker, P.6
  • 30
    • 0026551660 scopus 로고
    • Three dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution
    • Werner M. H., Wemmer D. E. Three dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution. Biochemistry. 31:1992;999-1010.
    • (1992) Biochemistry , vol.31 , pp. 999-1010
    • Werner, M.H.1    Wemmer, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.