Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii

Biochimie

Volumn 86, Issue 3, 2004, Pages 167-172

  Krauchenco, Sandra ^a   Nagem, Ronaldo A P ^a   Da Silva, José A ^b   Marangoni, Sérgio ^b   Polikarpov, Igor ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b UNIVERSITY OF CAMPINAS   (Brazil)

Author keywords

Trefoil fold; Copaifera langsdorffii; CTI; DrTI; ESI; Kunitz (STI) type trypsin inhibitor from Delonix regia seeds; Kunitz type trypsin inhibitor; Quick cryo soaking; trypsin inhibitor from Copaifera langsdorffii; X ray structure

Indexed keywords

APROTININ; TRYPSIN INHIBITOR;

ARTICLE; CHEMICAL STRUCTURE; COVALENT BOND; CRYSTAL STRUCTURE; DISULFIDE BOND; DRUG CONFORMATION; DRUG INHIBITION; PROTEIN FAMILY; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ALPHA-AMYLASE; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; FABACEAE; MODELS, MOLECULAR; PEPTIDES; PLANT PROTEINS; PROTEIN STRUCTURE, TERTIARY; TRYPSIN INHIBITORS;

COPAIFERA LANGSDORFFII; DELONIX REGIA; LOTUS;

EID: 2342625270     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.03.004     Document Type: Article

References (33)

1. Bode W., Huber R. Proteinase-protein inhibitor interaction. Biomed. Biochim. Acta. 50:1991;437-446
2. Laskowsky M. Jr, Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49:1980;593-626
3. Broadway R.M., Duffey S.S. The effect of plant protein quality on insect digestive physiology and the toxicity of plant proteinase inhibitors. J. Insect. Physiol. 34:1988;1111-1117
4. Yavelow J., Finlay T.H., Kennedy A.R., Troll W. Bowman-Birk soybean protease inhibitor as an anticarcinogen. Cancer Res. 43:1983;2454s-2459s
5. Billings P.C., Newberne P.M., Kennedy A.R. Protease inhibitor suppression of colon and anal gland carcinogenesis induced by dimethylhydrazine. Carcinogenesis. 11:1990;1083-1086
6. Billings P.C., Morrow A.R., Ryan C.A., Kennedy A.R. Inhibition of radiation-induced transformation of C3H/10T1/2 cells by carboxypeptidase inhibitor I and inhibitor II from potatoes. Carcinogenesis. 10:1989;687-691
7. Wlodawer A., Deisenhofer J., Huber R. Comparison of two highly refined structure of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 193:1987;145-156
8. Silva J.A., Macedo M.L.R., Novello J.C., Marangoni S. Biochemical characterization and N-terminal sequences of two new trypsin inhibitors from Copaifera langsdorffii seeds. J. Prot. Chem. 20:2001;1-7
9. Dauter Z., Dauter M., Rajashankar K.R. Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. Acta Crystallogr. D56:2000;232-237
10. Nagem R.A.P., Dauter Z., Polikarpov I. Protein crystal structure solution by fast incorporation of negatively and positively charged anomalous scatterers. Acta Crystallogr. D57:2001;996-1002
11. Krauchenco S., Silva J.A., Nagem R.A.P., Brandão Neto J.R., Forrer V.P., Carmona e Ferreira R. M.L.R. Macedo, J.C. Novello, S. Marangoni, I. Polikarpov, Crystallization and preliminary X-ray diffraction analysis of a novel trypsin inhibitor from seeds of Copaifera langsdorffii. Acta Crystallogr. D57:2001;1316-1318
12. Polikarpov I., Perles L.A., de Oliveira R.T., Oliva G., Castellano E.E., Garratt R., Craievich A. Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory. J. Synchrotron Rad. 5:1998;72-76
13. Polikarpov I., Teplyakov A., Oliva G. The ultimate wavelength for protein crystallography? Acta Crystallogr. D53:1997;734-737
14. Otwinowski Z., Minor W. Processing of X-ray data colleted in oscillation mode. Methods Enzymol. 276:1997;307-326
15. Weeks C.M., Miller R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32:1999;120-124
16. Blessing R.H., Smith G.D. Difference structure factor normalization for heavy-atom or anomalous-scattering substructure determinations. J. Appl. Crystallogr. 32:1999;664-670
17. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., Warren G.L. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D54:1998;905-921
18. de La Fortelle E., Bricogne G. Maximum-likelyhood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494
19. Collaborative Computational Project. Number 4, the CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50:1994;760-763
20. Perrakis A., Sixma T.K., Wilson K.S., Lamzin V.S. wARP: improvement and extension of crystallographic phases by weighted averaging of multiple refined dummy atomic models. Acta Crystallogr. D53:1997;448-455
21. Jones T.A., Bergdoll M., Kjeldgaard M. Bugg C., Ealick S. Crystallographic and Modelling Methods in Molecular Design. 1990;189-195 Springer-Verlag Press
22. Ramachandran G.N., Sasisekharan V. Stereochemistry of polypeptide chain configurations. Adv. Protein Chem. 23:1968;283-437
23. Murzin A.G., Lesk A.M., Chothia C. Beta-trefoil fold. J. Mol. Biol. 223:1992;531-543
24. McLachlan A.D. Three-fold structural pattern in the soybean trypsin inhibitor (Kunitz). J. Mol. Biol. 133:1979;557-563
25. Mukhopadhyay D. The molecular evolutionary history of a winged bean alpha-chymotrypsin inhibitor and modelling of its mutations through structural analyses. J. Mol. Evol. 50:2000;214-223
26. DiBella F.P., Liener I.E. Soybean trypsin inhibitor: cleavage and identification of a disulfide bridge not essential for activity. J. Biol. Chem. 244:1969;2824-2829
27. Lehle K., Wrba A., Jaenicke R. Erythrina trypsin inhibitor retains its native structure and function after reducing its disulfide groups. J. Mol. Biol. 239:1994;276-284
28. 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. 275:1998;347-363
29. Onesti S., Brick P., Blow D.M. Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds. J. Mol. Biol. 217:1990;153-176
30. Ravichandran S., Sen U., Chakrabarti C., Dattagupta J.K. Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K structure of a winged bean chymotrypsin inhibitor (WCI) at 2.13 Å resolution. Acta Crystallogr. D55:1999;1814-1821
31. Krauchenco S., Pando S.C., Marangoni S., Polikarpov I. Crystal structure of the Kunitz (STI) type inhibitor from Delonix regia seeds. Biochem. Biophys. Res. Commun. 312:2003;1303-1308
32. McCoy A.J., Kortt A.A. The 1.8 Å crystal structure of winged bean albumin 1, the major albumin from Psophocarpus tetragonolobus (L.) DC. J. Mol. Biol. 269:1997;881-891
33. Radisky E.S., Koshland D.E. Jr. A clogged gutter mechanism for protease inhibitors. Proc. Natl. Acad. Sci. USA. 99:2002;10316-10321