Human β-tryptase is a ring-like tetramer with active sites facing a central pore

Nature

Volumn 392, Issue 6673, 1998, Pages 306-311

  José Barbosa Pereira, Pedro ^a   Bergner, Andreas ^a   Macedo Ribeiro, Sandra ^a   Huber, Robert ^a   Matschiner, Gabriele ^b   Fritz, Hans ^b   Sommerhoff, Christian P ^b   Bode, Wolfram ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b LUDWIG MAXIMILIANS UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

SERINE PROTEINASE; TRYPTASE;

AMINO ACID SEQUENCE; ARTICLE; CRYSTALLIZATION; ENZYME ACTIVE SITE; HUMAN; HUMAN CELL; LUNG PARENCHYMA; MAST CELL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN PURIFICATION; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATTLE; CHYMASES; CRYSTALLOGRAPHY, X-RAY; ELECTROCHEMISTRY; HUMANS; LUNG; MAST CELLS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTASES;

EID: 2642600031     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/32703     Document Type: Article

References (30)

1. Caughey, G. H. Mast Cell Proteases in Immunology and Biology (Marcel Dekker, New York, 1995).
2. Caughey, G. H. Of mites and men: trypsin-like proteases in the lungs. Am. J. Respir. Cell Mol. Biol. 16, 621-628 (1997).
3. Seife, C. Blunting nature's swiss army knife. Science 277, 1602-1603 (1997).
4. Schwartz, L. B. et al. The alpha form of human tryptase is the predominant type present in blood at baseline in normal subjects and is elevated in those with systemic mastocytosis. J. Clin, Invest. 96, 2702-2710 (1995).
5. Sakai, K., Ren, S. & Schwartz, L. B. A novel heparin-dependent processing pathway for human tryptase. Autocatalysis followed by activation with dipeptidyl peptidase I. J. Clin. Invest. 97, 988-995 (1996).
6. Schwartz, L. B. Tryptase: a mast cell serine protcase. Methods Enzymol. 244, 88-100 (1994).
7. Alter, S. C., Metcalfe, D. D., Bradford, T. R. & Schwartz, L. B. Regulation of human mast cell tryptase Effects of enzyme concentration, ionic strength and the structure and negative charge density of polysaccharides. Biochem. J. 248, 821-827 (1987).
8. Schechter, N. M., Eng, G. Y. & McCaslin, D. R. Human skin tryptase: kinetic characterization of its spontaneous inactivation. Biochemistry 32, 2617-2625 (1993).
9. Addington, A. K. & Johnson, D. A. Inactivation of human lung tryptase: evidence for a re-activatable tetrameric intermediate and active monomers. Biochemistry 33, 13511-13518 (1996).
10. Sommerhoff, C. P. et al. A Kazal-type inhibitor of human mast cell tryptase; isolation from the medical leech Hirudo medicinalis characterization, and sequence analysis. Biol. Chem. Hoppe-Seyler 375, 685-694 (1994).
11. Stubbs, M. T. et al. The three dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin: implications for the structure of human mast cell tryptase and its inhibition. J. Biol. Chem. 272, 19931-19937 (1997).
12. Kam, G. M. et al. Mammalian tissue trypsin-like enzymes: substrate specificity and inhibitory potency of substituted isocoumarin mechanism-based inhibitors, benzamidine derivatives, and arginine fluoroalkyl ketone transition-state inhibitors. Arch. Biochem. Biophys. 316, 808-814 (1995).
13. Clark, J. M., Moore, W. R. & Tanaka, R. D. Tryptase inhibitors: a new class of antiinflammatory drugs. Drugs Future 21, 811-816 (1996).
14. Johnson, D. A. & Barton, G. T. Mast cell tryptases: examination of unusual characteristics by multiple sequence alignment and molecular modeling. Protein Sci. l, 370-377 (1992).
15. Matsumoto, R., Sali, A., Ghildyal, N., Karplus, M. & Stevens, R. L. Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells. A cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans. J. Biol. Chem, 270, 19524-19531 (1993).
16. Fujinaga, M., Chernaia, M. M., Halenbeck, R., Koths, K. & James, M. N. The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies. J. Mol. Biol. 261, 267-278 (1996).
17. Bode, W. & Schwager, P. The refined crystal structure of bovine bet a-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J. Mol. Biol. 98, 693-717 (1975).
18. Walter, J. & Bode, W. The X-ray crystal structure analysis of the refined complex formed by bovine trypsin and p-amidinophenylpyruvate at 1.4 Å resolution. Hoppe-Seyler's Z. Physoil. Chem. 364, 949-959 (1983).
19. Stürzebecher, J., Prasa, D. & Sommerhoff, C. P. Inhibition of human mast cell tryptase by benzamidine derivatives. Biol. Chem. Hoppe-Seyler 373, 1025-1030 (1992).
20. Caughey, G. H., Raymond, W. W., Bacci, E., Lombardy, R. J. & Tidwell, R. R. Bis(5-amidino-2-benzimidazolyl)methane and related amidines are potent, reversible inhibitors of mast cell tryptases. J. Pharmacol. Exp. Ther. 264, 676-682 (1993).
21. Fiorucci, L., Erba, F., Bolognesi, M., Coletta, M. & Ascoli, F. pH dependence of bovine mast cell tryptase catalytic activity and of its inhibition by 4',6-diamidino-2-phenylindole. FEBS Lett. 408, 85-88 (1997).
22. Bode, W. & Huber, R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204, 433-451 (1992).
23. Orwinowski, Z. & Minor, W. DENZO: a Film Processing for Macromolecular Crystallography (Yale Univ., 1993).
24. Navaza, J. An automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
25. Roussel, A. & Cambilleau, C. TurboFRODO in Sillicon Graphics Geometry (Sillicon Graphics, Mountain View, California, 1989).
26. Collaborative Computational Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
27. Brünger, G. J. XPLOR (version 3.1). A System for X-ray Crystallography and NMR (Yale Univ. Press, 1993).
28. Nicholls, A., Bharadwaj, R. & Honig, B. GRASP - graphical representation and analysis of surface properties. Biophys. J. 64, A166 (1993).
29. Barton, G. J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40 (1993).
30. Evans, S. V. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138 (1990).