Structure of rat procathepsin B: Model for inhibition of cysteine protease activity by the proregion

Structure

Volumn 4, Issue 4, 1996, Pages 405-416

  Cygler, Miroslaw ^a,b,c   Sivaraman, J ^a,b   Grochulski, Pawel ^a,c,d   Coulombe, René ^a,b   Storer, Andrew C ^a,b   Mort, John S ^b,e  

^a NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^b Networks of Centres of Excellence   (Canada)

^c Montreal Jt Ctr for Struct Biol   (Canada)

^d LODZ UNIVERSITY OF TECHNOLOGY   (Poland)

^e MCGILL UNIVERSITY   (Canada)

Author keywords

Cathepsin B; Cysteine protease; Procathepsin B; Proenzyme; Three dimensional structure

Indexed keywords

CATHEPSIN B; CYSTEINE PROTEINASE INHIBITOR; DRUG DERIVATIVE; ENZYME PRECURSOR; LEUCINE; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PROCATHEPSIN B; RECOMBINANT PROTEIN;

ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYME ACTIVATION; ENZYME SPECIFICITY; GENETICS; METABOLISM; PROTEIN CONFORMATION; RAT; X RAY CRYSTALLOGRAPHY;

ANIMALS; BINDING SITES; CATHEPSIN B; CRYSTALLOGRAPHY, X-RAY; CYSTEINE PROTEINASE INHIBITORS; ENZYME ACTIVATION; ENZYME PRECURSORS; LEUCINE; MODELS, MOLECULAR; PROTEIN CONFORMATION; RATS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0030584678     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00046-9     Document Type: Article

References (48)

1. Knop, M., Schiffer, H.H., Rupp, S. & Wolf, D.H. (1993). Vacuolar/lysosomal proteolysis: proteases, substrates, mechanisms. Curr. Opin. Cell Biol. 5, 990-996.
2. Takahashi, H., Cease, K.B. & Berzofsky, JA. (1989). Identification of proteases that process distinct epitopes on the same protein. J. Immunol. 142, 2221-2229.
3. Vaes, G. (1988). Cellular biology and biochemical mechanisms of bone resorption. A review of recent developments on the formation, activation and mode of action of osteoclasts. Clin. Orthop. 231, 239-271.
4. Sloane, B.F. & Honn, K.V. (1984). Cysteine proteinases and metastasis. Cancer Metastasis Rev. 3, 249-263.
5. Esser, R.E., et al., & Smith, R.E. (1994). Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis. Arthritis Rheum. 37, 236-247.
6. Neurath, H. (1989). Proteolytic processing and physiological regulation. Trends Biochem. Sci. 14, 268-271.
7. Fox, T., de Miguel, E., Mort, J.S. & Storer, A.C. (1992). Potent slow-binding inhibition of cathepsin B by its propeptide. Biochemistry 31, 12571-12576.
8. Taylor, M.A.J., et al., & Goodenough, P.W. (1995). Recombinant proregions from papain and papaya proteinase IV are selective high affinity inhibitors of the mature papaya enzymes. Protein Eng. 8, 59-62.
9. Tao, K., Stearns, N.A., Dong, J., Wu, Q. & Sahagian, G.G. (1994). The proregion of cathepsin L is required for proper folding, stability, and ER exit. Arch. Biochem. Biophys. 311, 19-27.
10. Mach, L., Mort, J.S. & Glössl, J. (1994). Non-covalent complexes between the lysosomal proteinase cathepsin B and its propeptide account for stable, extracellular, high molecular mass forms of the enzyme. J. Biol. Chem. 269, 13036-13040.
11. Gallagher, T., Gilliland, G., Wang, L & Bryan, P. (1995). The prosegment-subtilisin BNP' complex: crystal structure of a specific 'foldase'. Structure 3, 907-914.
12. Smith, S.M. & Gottesman, M. (1989). Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli. J. Biol. Chem. 264, 20487-20495.
13. Vernet, T., et al., & Thomas, D.Y. (1991). Processing of papain precursor. J. Biol. Chem. 266, 21451-21457.
14. Mach, L., Mort, J.S. & Glössl, J. (1994). Maturation of human cathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes. J. Biol. Chem. 269, 13030-13035.
15. Rowan, A.D., Mason, P., Mach, L. & Mort, J.S. (1992). Rat procathepsin B. Proteolytic processing to the mature form in vitro. J. Biol. Chem. 267, 15993-15999.
16. Kirschke, H. & Barrett, A.J. (1987). Chemistry of lysosomal proteases. In Lysosomes: Their role in protein breakdown. (Glaumann, H. & Ballard, F.J., eds), pp. 193-238, Academic Press, London.
17. Berti, P. & Storer, A.C. (1995). Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246, 273-283.
18. Karrer, K.M., Peiffer, S.L. & DiTomas, M.E. (1993). Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. USA 90, 3063-3067.
19. Huber, R. & Bode, W. (1978). Structural basis of the activation and action of trypsin. Accounts Chem. Res. 11, 114-122.
20. Bryan, P., et al.,. & Gallagher, T. (1995). Catalysis of a protein folding reaction: Mechanistic implications of a 2.0 Å structure of the subtilisin-prodomain complex. Biochemistry 34, 10310-10318.
21. James, M.N.G. & Sielecki, A.R. (1986). Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution. Nature 319, 33-38.
22. Coll, M., Guasch, A., Avilés, F.X. & Huber, R. (1991). Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its activity. EMBO J. 10, 1-9.
23. Becker, J.W., et al., & Springer, J.P. (1995). Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Prot. Sci. 4, 1966-1976.
24. Musil, D., et al., and Bode, W. (1991). The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity EMBO J. 10, 2321-2330.
25. Turk, D., et al., & Turk, V. (1995). Crystal structure of cathepsin B inhibited with CA030 at 2.0 Å resolution: A basis for the design of specific epoxysuccinyl inhibitors. Biochemistry 34, 4791-4797.
26. Jia, Z., et al., & Huber, C.P. (1995). Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex: implications for structure-based inhibitor design. J. Biol. Chem. 270, 5527-5533.
27. Baker, E.N. & Drenth, J. (1987). The thiol proteases: Structure and mechanism. In Biological Macromolecules and Assemblies, Vol. 3. (Jurnak, FA. & McPherson, A. eds), pp. 313-368, John Wiley & Sons, New York.
28. Moore, S.A., Sielecki, A.R., Chernaia, M.M., Tarasova, N.I. & James, M.N.G. (1995). Crystal and molecular structures of human progastricsin at 1.62 Å resolution. J. Mol. Biol. 247, 466-485.
29. Hasnain, S., Hirama, T., Huber, C.P., Mason, P. & Mort, J.S. (1993). Characterization of cathepsin B specificity by site-directed mutagenesis. Importance of Glu245 in the S2-P2 specificity for arginine and its role in transition state stabilization. J. Biol. Chem. 268, 235-240.
30. Khouri, H.E., et al., & Storer, A.C. (1991). Engineering of papain: selective alteration of substrate specificity by site-directed mutagenesis. Biochemistry 30, 8929-8936.
31. Feng, S.B., Chen, J.K., Yu, H.T., Simon, J.A & Schreiber, S.L. (1994). Two binding orientations for peptides to the src SH3 domain - development of a general model for SH3-ligand interactions. Science 266, 1241-1247.
32. Varughese, K.I., Su, Y., Cromwell, D., Hasnain, S. & Xuong, N.H. (1992). Crystal structure of an actinidin-E-64 complex. Biochemistry 31, 5172-5176.
33. . Varughese, K.I., et al., & Storer, A.C. (1989). Crystal structure of papain-E-64 complex. Biochemistry 28, 1330-1332.
34. Yamamoto, D., et al., & Mizuno, H. (1991). Refined x-ray structure of papain-E-64-c complex at 2.1 Å resolution. J. Biol. Chem. 266, 14771-14777.
35. Kim, M.J., et al., & Kitamura, K. (1992). Crystal structure of papain-E64-c complex. Binding diversity of E64-C to papain S2 and S3 subsites. Biochem. J. 287, 797-803.
36. Gour-Salin, B.J., et al., & Storer, A.C. (1995). E-64 [transepoxysuccinyl-L-leucylamido-(4-guanidino)butane] analogues as inhibitors of cysteine proteinases: investigation of S2 subsite interactions. Biochem. J. 299, 389-392.
37. Guasch, A., Coll, M., Aviles, F.X. & Huber, R. (1992). Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation. J. Mol. Biol. 224, 141-157.
38. Rydel, TJ., et al., & Fenton, J.W. Jr. (1990). The structure of a complex of recombinant hirudin and human α-thrombin. Science 249, 277-280.
39. DiMaio, J., et al., & Konishi, Y. (1 990). Bifunctional thrombin inhibitors based on the sequence of hirudin. J. Biol. Chem. 265, 21698-21703.
40. San Segundo, B., Chan, S.J. & Steiner, D.F. (1985). Identification of cDNA clones encoding a precursor of rat liver cathepsin B. Proc. Nat. Acad. Sci. USA 82, 2320-2324.
41. Sivaraman, J., et al., & Cygler, M. (1996). Crystallization of rat procathepsin B. Acta Cryst. D, in press.
42. Navaza J. (1994). AMoRe: an automated package for molecular replacement. Acta. Cryst. 50, 157-163.
43. Brünger, AT. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
44. Kleywegt, G.J. & Jones, T.A. (1994) Halloween... Masks and Bones. In From first map to final model. (Bayley. S., Hubbard R. & Waller D., eds), pp.59-66, SERC Daresbury Laboratory, Daresbury, England.
45. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
46. Laskowski, R.A., MacArthur, M.W., Moss D.S. & Thornton J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
47. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
48. Nicholls, A., Sharp, K. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.