Crystallization and preliminary X-ray diffraction studies of human procathepsin L

Proteins: Structure, Function and Genetics

Volumn 25, Issue 3, 1996, Pages 398-400

  Coulombe, René ^a,b,d   Li, Yunge ^b,d   Takebe, Sachiko ^a,d   Ménard, Robert ^a,d   Mason, Patrizia ^c   Mort, John S ^a,c   Cygler, Miroslaw ^a,b,d  

^a Networks of Centres of Excellence   (Canada)

^b Montreal Jt Ctr for Struct Biol   (Canada)

^c MCGILL UNIVERSITY   (Canada)

^d NATIONAL RESEARCH COUNCIL CANADA   (Canada)

Author keywords

crystallization; cysteine protease; procathepsin L; proenzyme; purification

Indexed keywords

BUFFER; CATHEPSIN L; ENZYME PRECURSOR;

ARTICLE; CRYSTALLIZATION; DIFFUSION; ENDOMYCETALES; GLYCOSYLATION; PRIORITY JOURNAL; X RAY DIFFRACTION;

EID: 0029742220     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199607)25:3<398::AID-PROT11>3.3.CO;2-R     Document Type: Article

References (21)

1. Knop, M., Schiffer, H.H., Rupp, S., Wolf, D.H. Vacuolar/ lysosomal proteolysis: Proteases, substrates, mechanisms. Curr. Opin. Cell Biol. 5:990-996, 1993.
2. Takahashi, H., Cease, K.B., Berzofsky, J.A. Identification of proteases that process distinct epitopes on the same protein. J. Immunol. 142:2221-2229, 1989.
3. Vaes, G. 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, 1988.
4. Sloane, B.F., Honn, K.V. Cysteine proteinases and metastasis. Cancer Metas. Rev. 3:249-263, 1984.
5. Esser, R.E., Angelo, R.A., Murphey, M.D., Watts, L.M., Thornburg, L.P., Palmer, J.T., Talhouk, J.W., Smith, R.E. Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis. Arthritis Rheum. 37:236-247, 1994.
6. Neurath, H. Proteolytic processing and physiological regulation. TIBS 14:268-271, 1989.
7. Fox, T., de Miguel, E., Mort, J.S., Storer, A.C. Potent slow-binding inhibition of cathepsin B by its propeptide. Biochemistry 31:12571-12576, 1992.
8. Tao, K., Stearns, N.A., Dong, J., Wu, Q., Sahagian, G.G. The proregion of cathepsin L is required for proper folding, stability, and ER exit. Arch. Biochem. Biophys. 311:19-27, 1994.
9. Mach, L., Mort, J.S., Glössl, J. 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, 1994.
10. Mach, L., Mort, J.S., Glössl, J. 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, 1994.
11. Huber, R., Bode, W. Structural basis of the activation and action of trypsin. Accounts Chem. Res. 11:114-122, 1978.
12. Bryan, P., Wang, L., Hoskins, J., Ruvinov, S., Strausberg, S., Alexander, P., Almog, O., Gilliland, G., Gallagher, T. Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex. Biochemistry 34:10310-10318, 1995.
13. James, M.N.G., Sielecki, A.R. Molecular structure of an aspartic proteinase xymogen, porcine pepsinogen, at 1.8 Å resolution. Nature 319:33-38, 1986.
14. Coll, M., Guasch, A., Avilés, F.X., Huber, R. Three-dimensional structure of porcine procarboxypeptidase B: A structural basis of its activity. EMBO J. 10:1-9, 1991.
15. Vernet, T., Dignard, D., thomas, D.Y. A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52:225-233, 1987.
16. Kunkel, T.A., Roberts, J.D., Zakour, R.A. Rapid and efficient site-directed mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382, 1987.
17. Jancarik J., Kim, S.H. Sparse matrix sampling: A screening method for crystallization of proteins. J. Appl. Crystallogr. 24:409-411, 1991.
18. Sakabe N. X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl Inst Methods Phys Res A303:448-463, 1991.
19. Drenth, J., Jansonius, J.N. Koekoek, R., Swen, H.M., Wolthers, B.G. Structure of papain. Nature 218:929, 1968.
20. Baker, E.N. Structure of actinidin. Details of the polypeptide chain conformation and active site from an electron density map at 2.8 angstroms resolution. J. Mol. Biol. 115: 263, 1977.
21. Pickersgill, R.W. Rizkallah, P., Harris, G.W., Goodenough, P.W. Determination of the structure of papaya protease omega. Acta Crystallogr. B47:766, 1991.