Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2

Biochemistry

Volumn 44, Issue 18, 2005, Pages 6823-6830

  Radisky, Evette S ^a   Lu, Chia Jung Karen ^a   Kwan, Gene ^a,b   Koshland Jr , Daniel E ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; CRYSTAL STRUCTURE; ENZYMES; HYDROGEN BONDS; MOLECULAR STRUCTURE;

CHYMOTRYPSIN INHIBITOR 2 (CI2); INTERMOLECULAR HYDROGEN BOND NETWORK; INTERMOLECULAR INTERACTIONS; MUTANTS; PROTEOLYSIS;

BIOCHEMISTRY;

ARGININE; CHYMOTRYPSIN INHIBITOR; CHYMOTRYPSIN INHIBITOR 2; GLUTAMIC ACID; GLYCINE; SERINE PROTEINASE; THREONINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME INHIBITION; ENZYME STABILITY; HYDROGEN BOND; HYDROLYSIS; MOLECULAR INTERACTION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; STRUCTURE ANALYSIS;

ARGININE; BACILLUS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; GLUTAMIC ACID; HORDEUM; HYDROGEN BONDING; HYDROLYSIS; METHIONINE; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PLANT PROTEINS; PROTEIN BINDING; SERINE; SERINE PROTEINASE INHIBITORS; SOLVENTS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBTILISINS; THREONINE;

EID: 18244402180     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047301w     Document Type: Article

References (33)

1. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., and Bourne, P. E. (2000) The protein data bank, Nucleic Acids Res. 28, 235-242.
2. Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain, Biochem. Biophys. Res. Commun. 27, 157-162.
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. 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.
5. Radisky, E. S., Kwan, G., Lu, C. K., and Koshland, D. E., Jr. (2004) Binding, proteolytic, and crystallographic analyses of mutations at the protease/inhibitor interface of the subtilisin BPN′/chymotrypsin inhibitor 2 complex, Biochemistry 43, 13648-13656.
6. 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.
7. McPhalen, C. A., and James, M. N. G. (1988) Structural comparison of two serine proteinase-protein inhibitor complexes: Eglin-c-subtilisin Carlsberg and CI-2-subtilisin novo, Biochemistry 27, 6582-6598.
8. 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.
9. Heinz, D. W., Hyberts, S. G., Peng, J. W., Priestle, J. P., Wagner, G., and Grütter, M. G. (1992) Changing the inhibitory specificity and function of the proteinase inhibitor eglin c by site-directed mutagenesis: Functional and structural investigation, Biochemistry 31, 8755-8766.
10. Holton, J., and Alber, T. (2004) Automated protein crystal structure determination using ELVES, Proc. Natl. Acad. Sci. U.S.A. 101, 1537-1542.
11. Leslie, A. G. W. (1992) Recent changes to the MOSFLM package for processing film and image plate data, Joint CCP4+ESF-EAMCB Newsletter on Protein Crystallography 26.
12. Collaborative Computational Project Number 4 (1994) The CCP4 suite: Programs for protein crystallography, Acta Crystallogr. D50, 760-763.
13. Kissinger, C. R., Gehlhaar, D. K., and Fogel, D. B. (1999) Rapid automated molecular replacement by evolutionary search, Acta Crystallogr. D55, 484-491.
14. 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.
15. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallogr. D53, 240-255.
16. Perrakis, A., Morris, R., and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement, Nat. Struct. Biol. 6, 458-463.
17. Hooft, R. W. W., Vriend, G., Sander, C., and Abola, E. E. (1996) Errors in protein structures, Nature 381, 272.
18. Fauman, E. B., Rutenber, E. E., Maley, G. F., Maley, F., and Stroud, R. M. (1994) Water-mediated substrate/product discrimination: The product complex of thymidylate synthase at 1.83 Å, Biochemistry 33, 1502-1511.
19. Otzen, D. E., and Fersht, A. R. (1999) Analysis of protein - protein interactions by mutagenesis: Direct versus indirect effects, Protein Eng. 12, 41-45.
20. Rawlings, N. D., Tolle, D. P., and Barrett, A. J. (2004) MEROPS: The peptidase database, Nucleic Acids Res. 32 (Database Issue), D160-D164.
21. 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.
22. 52 in Curcurbita maxima trypsin inhibitor-V deduced by trypsin-catalyzed hydrolysis and NMR spectroscopy, Biochemistry 35, 4784-4794.
23. Cai, M., Gong, Y.-X., Wen, L., and Krishnamoorthi, R. (2002) Correlation of binding-loop internal dynamics with stability and function in the potato I inhibitor family: Relative contributions of Arg50 and Arg52 in Curcurbita maxima trypsin inhibitor-V as studied by site-directed mutagenesis and NMR spectroscopy, Biochemistry 41, 9572-9579.
24. Boisen, S., Andersen, C. Y., and Hejgaard, J. (1981) Inhibitors of chymotrypsin and microbial serine proteases in barley grains, Physiol. Plant. 52, 167-176.
25. Jonassen, I., and Svendsen, I. (1982) Identification of the reactive sites in two homologous serine proteinase inhibitors isolated from barley, Carlsberg Res. Commun. 47, 199-203.
26. Li, Y., Huang, Q., Zhang, S., Liu, S., Chi, C., and Tang, Y. (1994) 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, 18-25.
27. Luckett, S., Garcia, R. S., Barker, J. J., Konarev, Al. V., Shewry, P. R., Clarke, A. R., and Brady, R. L. (1999) High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds, J. Mol. Biol. 290, 525-533.
28. 2 variation in cyclic peptides encompassing the reactive site loop, J. Mol. Biol. 282, 447-457.
29. Fujinaga, M., Read, R. J., Sielecki, A., Ardelt, W., Laskowski, M., Jr., and James, M. N. G. (1982) Refined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey, Proc. Natl. Acad. Sci. U.S.A. 79, 4868-4872.
30. Papamokos, E., Weber, E., Bode, W., Huber, R., Empie, M. W., Kato, I., and Laskowski, M., Jr. (1982) Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases, J. Mol. Biol. 158, 515-537.
31. 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.
32. 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.
33. 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.