Spacer Asn determines the fate of Kunitz (STI) inhibitors, as revealed by structural and biochemical studies on WCI mutants

Biochemistry

Volumn 45, Issue 22, 2006, Pages 6783-6792

  Dasgupta, Jhimli ^a   Khamrui, Susmita ^a   Dattagupta, Jiban K ^a   Sen, Udayaditya ^a  

^a SAHA INSTITUTE OF NUCLEAR PHYSICS   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; ENZYMES; MUTAGENESIS; SUBSTRATES;

KUNITZ (STI) INHIBITORS; PROTEOLYSIS; SERINE PROTEASE INHIBITORS; WINGED BEAN CHYMOTRYPSIN INHIBITOR (WCI);

BIOCHEMISTRY;

ALANINE; APROTININ; ASPARAGINE; CHYMOTRYPSIN INHIBITOR; GLYCINE; LEUCINE; PROTEINASE; SERINE PROTEINASE INHIBITOR; SPACER ASPARAGINE; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL BOND; DATA ANALYSIS; DATA BASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARAGINE; CHYMOTRYPSIN; MOLECULAR SEQUENCE DATA; MUTATION; PLANT PROTEINS; PROTEIN CONFORMATION;

PSOPHOCARPUS TETRAGONOLOBUS;

EID: 33744958385     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060374q     Document Type: Article

References (36)

1. Laskowski, M., Jr., and Kato, I. (1980) Protein inhibitors of proteinases, Annu. Rev. Biochem. 49, 593-626.
2. Bode, W., and Huber, R. (1992) Natural protein proteinase inhibitors and their interaction with proteinases, Eur. J. Biochem. 204, 433-451.
3. 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.
4. 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? Biochem. Biophys. Acta 1477, 324-337.
5. Dattagupta, J. K., Podder, A., Chakrabarti, C., Sen, U., Dutta, S. K., and Singh, M. (1996) Structure=of a Kunitz-type chymotrypsin from winged bean seeds at 2.95 Å resolution, Acta Crystallogr. D52, 521-528.
6. Song, H., K., and Suh, S., W. (1998) 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, 347-363.
7. Radisky, E. S., Lu, C. J., Kwan, G., and Koshland, D. E., Jr. (2005) Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2, Biochemistry 44, 6823-6830.
8. Radisky, E. S., King, D. S., Kwan, G., and Koshland, D. E., Jr. (2003) The role of the protein core in the inhibitory power of the classic serine protease inhibitor, chymotrypsin inhibitor 2, Biochemistry 42, 6484-6492.
9. Radisky, E. S., Kwa, G., Karen, Lu, C. J., and Koshland, D. E., Jr. (2004) Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN7 chymotrypsin inhibitor 2 complex, Biochemistry 43, 13648-13656.
10. Onesti, S., Brick, P., and Blow, D. M. (1991) Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds, J. Mol. Biol. 217, 153-176.
11. Meester, P. De, Brick, P., Lloyd, L. F., Blow, M. D., and Onesti, S. (1998) Structure of the Kunitz-type soybean trypsin inhibitor (STI): implication for the interactions between members of the STI family and tissue-plasminogen activator, Acta Crystallogr. D54, 589-597.
12. Dattagupta, J. K., Podder, A., Chakrabarti, C., Sen, U., Mukhopadhyay, D., Dutta, S. K., and Singh, M. (1999) Refined crystal structure (2.3 Å of a double-headed winged bean alpha-chymotrypsin inhibitor and location of its second reactive site, Proteins: Struct. Funct., Genet. 35, 321-331.
13. Ravichandran, S., Dasgupta, J., Chakrabarti, C., Ghosh, S., Singh, M., and Dattagupta, J., K. (2001) The role of Asn14 in the stability and conformation of the reactive-site loop of winged bean chymotrypsin inhibitor: crystal structures of two point mutants Asn14 → Lys and Asn14 → Asp, Protein Eng. 14, 349-357.
14. Dasgupta, J., Sen, U., and Dattagupta, J. K. (2003) In silico mutations and molecular dynamics studies on a winged bean chymotrypsin inhibitor protein, Protein Eng. 16, 489-496.
15. Khamrui, S., Dasgupta, J., Dattagupta, J. K., and Sen, U. (2005) Single mutation at P1 of a chymotrypsin inhibitor changes it to a trypsin inhibitor: X-ray structural (2.15 Å) and biochemical basis, Biochim. Biophys. Acta 1752, 65-72.
16. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
17. Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D50, 760-763.
18. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination, Acta Crystallogr. D54, 905-921.
19. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
20. Walsh, K. A., and Wilcox, P. E. (1970) Serine proteases, Methods Enzymol. 19, 31-41.
21. Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
22. Merritt, E. A., and Bacon, D. J. (1997) Raster3D: Photorealistic Molecular Graphics, Methods Enzymol. 277, 505-524.
23. Fraczkiewicz, R., and Braun, W. (1998) Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules, J. Comput. Chem. 19, 319-333.
24. Kortt, A. A. (1980) Isolation and properties of a chymotrypsin inhibitor from winged bean seed (Psophocarpus tetragonolobus (L) Dc.), Biochim. Biophys. Acta 624, 237-248.
25. Bieth, J. G. (1995) Theoretical and practical aspects of proteinase inhibition kinetics, Methods Enzymol. 248, 59-84.
26. Bode, W., Epp, O., Huber, R, Laskowski, M., Jr., and Ardelt, W. (1985) The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3), Eur. J. Biochem. 147, 387-395.
27. Hecht, H. J., Szardenings, M., Collins, J., and Schomburg, D. (1992) Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (Kazal type), J. Mol. Biol. 225, 1095-1103.
28. Maynes, J. T., Cherney, M. M., Qasim, M. A., Laskowski, M., Jr., and James, M. N. G. (2005) Structure of the subtilisin Carlsberg-OMTKY3 complex reveals two different ovomucoid conformations, Acta Crystallogr. D-Biol. Crystallogr. 61, 580-588.
29. van de Locht, A., Lamba, D., Bauer, M., Huber, R., Friedrich, T., Kroger, B., Hoffken, W., and Bode, W. (1995) Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin, EMBO J. 14, 5149-5157.
30. Eggers, C. T., Wang, S. X., Fletterick, R. J., and Craik, C. S. (2001) The role of ecotin dimerization in protease inhibition, J. Mol. Biol. 308, 975-991.
31. Takeuchi, Y., Satow, Y., Nakamura, K. T., and Mitsui, Y. (1991) Refined crystal structure of the complex of subtilisin BPN′ and Streptomyces subtilisin inhibitor at 1.8 Å resolution, J. Mol. Biol. 221, 309-325.
32. Roussel, A., Mathieu, M., Dobbs, A., Luu, B., Cambillau, C., and Kellenberger, C. (2001) Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity, J. Biol. Chem. 276, 38893-38898.
33. Fodor, K., Harmat, V., Hetenyi, C., Kardos, J., Antal, J., Perczel, A., Patthy, A., Katona, G., and Graf, L. (2005) Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition, J. Mol. Biol. 350, 151-169.
34. Greenblatt, H. M., Ryan, C. A., and James, M. N. (1989) Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 Å resolution, J. Mol. Biol. 205, 201-228.
35. Barrette-Ng, I. H., Ng, K. K., Cherney, M. M., Pearce, G., Ghani, U., Ryan, C., A., and James, M. N. (2003) Unbound form of tomato inhibitor-II reveals interdomain flexibility and conformational variability in the reactive site loops, J. Biol. Chem. 278, 31391-31400.
36. Rawlings, N. D., Tolle, D. P., and Barrett, A. J. (2004) MEROPS: the peptidase database, Nucleic Acids Res. 32, D160-D164.