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Volumn 293, Issue 5, 1999, Pages 1133-1144

Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 Å resolution

Author keywords

Bowman Birk trypsin inhibitor; Double headed inhibitor; Gene duplication; Monocotyledonous plant; Reactive site loop

Indexed keywords

ARGININE; BOWMAN BIRK INHIBITOR; TRYPSIN INHIBITOR;

EID: 0033550195     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3239     Document Type: Article
Times cited : (56)

References (47)
  • 1
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G. J. 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
  • 2
    • 0000680174 scopus 로고
    • Proteinase inhibitors
    • A. Neuroberger, & K. Brocklehurst. Amsterdam: Elsevier Science Publishers B.V.
    • Birk Y. Proteinase inhibitors. Neuroberger A., Brocklehurst K. Hydrolytic Enzymes. 1987;257-300 Elsevier Science Publishers B.V. Amsterdam.
    • (1987) Hydrolytic Enzymes , pp. 257-300
    • Birk, Y.1
  • 3
    • 0002733513 scopus 로고
    • Protease inhibitors of plant origin and role of protease inhibitors in human nutrition
    • W. Troll, & A. R. Kennedy. New York: Plenum Press
    • Birk Y. Protease inhibitors of plant origin and role of protease inhibitors in human nutrition. Troll W., Kennedy A. R. Protease Inhibitors as Cancer Chemopreventive Agents. 1993;97-106 Plenum Press, New York.
    • (1993) Protease Inhibitors As Cancer Chemopreventive Agents , pp. 97-106
    • Birk, Y.1
  • 4
    • 0000835634 scopus 로고
    • A pure trypsin inhibitor from soya beans
    • Birk Y., Gertler A., Khalef S. A pure trypsin inhibitor from soya beans. Biochem. J. 87:1963;281-284.
    • (1963) Biochem. J. , vol.87 , pp. 281-284
    • Birk, Y.1    Gertler, A.2    Khalef, S.3
  • 5
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interactions with proteinases
    • Bode W., Huber R. Natural protein proteinase inhibitors and their interactions with proteinases. Eur. J. Biochem. 204:1992;433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 6
    • 84986802647 scopus 로고
    • Protease inhibitor from barley embryo inhibiting trypsin and trypsin-like microbial proteases. Purification and characterization of two isoforms
    • Boisen S., Djurtoft R. Protease inhibitor from barley embryo inhibiting trypsin and trypsin-like microbial proteases. Purification and characterization of two isoforms. J. Sci. Food Agric. 33:1982;431-440.
    • (1982) J. Sci. Food Agric. , vol.33 , pp. 431-440
    • Boisen, S.1    Djurtoft, R.2
  • 7
    • 84956475337 scopus 로고
    • Differentiation of soy bean anti-tryptic factors
    • Bowman D. E. Differentiation of soy bean anti-tryptic factors. Proc. Soc. Expt. Biol. Med. 63:1946;547-550.
    • (1946) Proc. Soc. Expt. Biol. Med. , vol.63 , pp. 547-550
    • Bowman, D.E.1
  • 10
    • 0026526805 scopus 로고
    • Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors
    • Chen P., Rose J., Love R., Wei C. H., Wang B.-C. Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors. J. Biol. Chem. 267:1992;1990-1994.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1990-1994
    • Chen, P.1    Rose, J.2    Love, R.3    Wei, C.H.4    Wang, B.-C.5
  • 11
    • 0031058188 scopus 로고    scopus 로고
    • Maxium-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle E., Bricogne G. Maxium-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 12
    • 0001483373 scopus 로고    scopus 로고
    • Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds
    • de la Sierra I. L., Quillien L., Flecker P., Gueguen J., Brunie S. Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds. J. Mol. Biol. 285:1999;1195-1207.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1195-1207
    • De La Sierra, I.L.1    Quillien, L.2    Flecker, P.3    Gueguen, J.4    Brunie, S.5
  • 13
    • 0029096631 scopus 로고
    • Template-directed protein folding into a metastable state of increased activity
    • Flecker P. Template-directed protein folding into a metastable state of increased activity. Eur. J. Biochem. 232:1995;528-535.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 528-535
    • Flecker, P.1
  • 15
    • 0018348545 scopus 로고
    • Trypsin inhibitory activity of a polypeptide isolated from red kidney beans that also enhances lymphocyte stimulation
    • Harms-Ringdahl M., Forsberg J., Fedorcsák I., Ehrenberg L. Trypsin inhibitory activity of a polypeptide isolated from red kidney beans that also enhances lymphocyte stimulation. Biochem. Biophys. Res. Commun. 86:1979;492-499.
    • (1979) Biochem. Biophys. Res. Commun. , vol.86 , pp. 492-499
    • Harms-Ringdahl, M.1    Forsberg, J.2    Fedorcsák, I.3    Ehrenberg, L.4
  • 16
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multiwavelength anomalous diffraction measurements
    • Hendrickson W. A., Ogata C. M. Phase determination from multiwavelength anomalous diffraction measurements. Methods Enzymol. 276:1997;494-523.
    • (1997) Methods Enzymol. , vol.276 , pp. 494-523
    • Hendrickson, W.A.1    Ogata, C.M.2
  • 17
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 18
    • 0032512619 scopus 로고    scopus 로고
    • Rapid refinement of protein interfaces incorporating solvation: Application to the docking problem
    • Jackson R. M., Gabb H. A., Sternberg M. J. E. Rapid refinement of protein interfaces incorporating solvation: application to the docking problem. J. Mol. Biol. 276:1998;265-285.
    • (1998) J. Mol. Biol. , vol.276 , pp. 265-285
    • Jackson, R.M.1    Gabb, H.A.2    Sternberg, M.J.E.3
  • 19
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions derived from structural studies
    • Jones S., Thornton J. M. Principles of protein-protein interactions derived from structural studies. Proc. Natl Acad. Sci. USA. 93:1996;13-20.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 20
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron-density maps and the location of error in these maps
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for the building of protein models in electron-density maps and the location of error in these maps. 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
  • 21
    • 0003025605 scopus 로고
    • Anticarcinogenic activity of protease inhibitors
    • W. Troll, & A. R. Kennedy. New York: Plenum Press
    • Kennedy A. R. Anticarcinogenic activity of protease inhibitors. Troll W., Kennedy A. R. Protease Inhibitors as Cancer Chemopreventive Agents. 1993;9-64 Plenum Press, New York.
    • (1993) Protease Inhibitors As Cancer Chemopreventive Agents , pp. 9-64
    • Kennedy, A.R.1
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. 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
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., 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
  • 24
    • 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. (Tokyo). 116:1994;18-25.
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 18-25
    • Li, Y.1    Huang, Q.2    Zhang, S.3    Liu, S.4    Chi, C.5    Tang, Y.6
  • 25
    • 0027409046 scopus 로고
    • The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin
    • Lin G., Bode W., Huber R., Chi C., Engh R. A. The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin. Eur. J. Biochem. 212:1993;549-555.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 549-555
    • Lin, G.1    Bode, W.2    Huber, R.3    Chi, C.4    Engh, R.A.5
  • 28
    • 0000557591 scopus 로고
    • Differences between endospermal and embryonal trypsin inhibitors in barley, wheat, and rye
    • Mikola J., Kirsi M. Differences between endospermal and embryonal trypsin inhibitors in barley, wheat, and rye. Acta Chem. Scand. 26:1972;787-795.
    • (1972) Acta Chem. Scand. , vol.26 , pp. 787-795
    • Mikola, J.1    Kirsi, M.2
  • 31
    • 0021099669 scopus 로고
    • The complete amino acid sequences of barley trypsin inhibitor
    • Odani S., Koide T., Ono T. The complete amino acid sequences of barley trypsin inhibitor. J. Biol. Chem. 258:1983;7998-8003.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7998-8003
    • Odani, S.1    Koide, T.2    Ono, T.3
  • 33
    • 0025977085 scopus 로고
    • Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds
    • Onesti S., Brick P., Blow D. M. Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds. J. Mol. Biol. 217:1991;153-176.
    • (1991) J. Mol. Biol. , vol.217 , pp. 153-176
    • Onesti, S.1    Brick, P.2    Blow, D.M.3
  • 34
    • 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
  • 35
    • 0032005175 scopus 로고    scopus 로고
    • Mutational analysis of disulfide bonds in the trypsin-reactive subdomain of a Bowman-Birk-type inhibitor of trypsin and chymotrypsin. Cooperative versus autonomous refolding of subdomains
    • Philipp S., Kim Y.-M., Dürr I., Wenzl G., Vogt M., Flecker P. Mutational analysis of disulfide bonds in the trypsin-reactive subdomain of a Bowman-Birk-type inhibitor of trypsin and chymotrypsin. Cooperative versus autonomous refolding of subdomains. Eur. J. Biochem. 251:1998;854-862.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 854-862
    • Philipp, S.1    Kim, Y.-M.2    Dürr, I.3    Wenzl, G.4    Vogt, M.5    Flecker, P.6
  • 37
    • 0031045818 scopus 로고    scopus 로고
    • Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement
    • Ramakrishnan V., Biou V. Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement. Methods Enzymol. 276:1997;538-557.
    • (1997) Methods Enzymol. , vol.276 , pp. 538-557
    • Ramakrishnan, V.1    Biou, V.2
  • 38
    • 0003150431 scopus 로고
    • Introduction to protein inhibitors: X-ray crystallography
    • A. J. Barrett, & G. Salvesen. Amsterdam: Elsevier
    • Read R. J., James M. N. G. Introduction to protein inhibitors: X-ray crystallography. Barrett A. J., Salvesen G. Proteinase Inhibitors. 1986;301-335 Elsevier, Amsterdam.
    • (1986) Proteinase Inhibitors , pp. 301-335
    • Read, R.J.1    James, M.N.G.2
  • 39
    • 0000082544 scopus 로고
    • CHAIN - A crystallographic modeling program
    • Sack J. S. CHAIN - a crystallographic modeling program. J. Mol. Graph. 6:1988;244-245.
    • (1988) J. Mol. Graph. , vol.6 , pp. 244-245
    • Sack, J.S.1
  • 40
    • 0032536108 scopus 로고    scopus 로고
    • Kunitz-type soybean trypsin inhibitor revisited: Refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator
    • Song H. K., Suh S. W. Kunitz-type soybean trypsin inhibitor revisited: Refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. J. Mol. Biol. 275:1998a;347-363.
    • (1998) J. Mol. Biol. , vol.275 , pp. 347-363
    • Song, H.K.1    Suh, S.W.2
  • 41
    • 0032078075 scopus 로고    scopus 로고
    • Preliminary X-ray crystallographic analysis of Bowman-Birk trypsin inhibitor from barley seeds
    • Song H. K., Suh S. W. Preliminary X-ray crystallographic analysis of Bowman-Birk trypsin inhibitor from barley seeds. Acta Crystallog. sect. D. 54:1998b;441-443.
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 441-443
    • Song, H.K.1    Suh, S.W.2
  • 42
    • 0027139339 scopus 로고
    • Crystallographic refinement of Bowman-Birk type protease inhibitor A-II from peanut (Arachis hypogaea) at 2.3 Å resolution
    • Suzuki A., Yamane T., Ashida T., Norioka S., Haram S., Ikenazka T. Crystallographic refinement of Bowman-Birk type protease inhibitor A-II from peanut (Arachis hypogaea) at 2.3 Å resolution. J. Mol. Biol. 234:1993;722-734.
    • (1993) J. Mol. Biol. , vol.234 , pp. 722-734
    • Suzuki, A.1    Yamane, T.2    Ashida, T.3    Norioka, S.4    Haram, S.5    Ikenazka, T.6
  • 43
    • 0025038757 scopus 로고
    • The complete amino acid sequence of a major trypsin inhibitor from seeds of foxtail millet (Setaria italica)
    • Tashiro M., Asao T., Hirata C., Takahashi K., Kanamoru M. The complete amino acid sequence of a major trypsin inhibitor from seeds of foxtail millet (Setaria italica). J. Biochem. (Tokyo). 108:1990;669-672.
    • (1990) J. Biochem. (Tokyo) , vol.108 , pp. 669-672
    • Tashiro, M.1    Asao, T.2    Hirata, C.3    Takahashi, K.4    Kanamoru, M.5
  • 46
    • 0029658121 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution
    • Voss R.-H., Ermler U., Essen L.-O., Wenzl G., Kim Y.-M., 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.-H.1    Ermler, U.2    Essen, L.-O.3    Wenzl, G.4    Kim, Y.-M.5    Flecker, P.6
  • 47
    • 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


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