Structure of the complex of bovine pancreatic phospholipase A2 with a transition-state analogue

Acta Crystallographica Section D: Biological Crystallography

Volumn 54, Issue 3, 1998, Pages 334-341

  Sundaralingam, Muttaiya ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOLIPASE A;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; MOLECULAR GENETICS; PANCREAS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CATTLE; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PANCREAS; PHOSPHOLIPASES A;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0032077157     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S090744499701247X     Document Type: Article

References (18)

1. Brünger, A. T. (1992). X-PLOR Version 3.1. A system for X-ray crystallography and NMR. New Haven, Connecticut, USA.
2. Cha, S.-S., Lee, D., Adams, J., Kurdyla, J. T., Jones, C. S., Marshall, L. A., Bolognese, B., Abdel-Meguid, S. S. & Oh, B.-H. (1996). J. Med. Chem. 30, 3878-3881.
3. Dijkstra, B. W., Drenth, J. & Kalk, K. H. (1981). Nature (London), 289, 604-606.
4. Howard, A. J. (1990). A guide to macromolecular X-ray data reduction for the Siemens area detector system. The XENGEN system, version 2.0, Genex Corporation, Gaithersburg, Maryland, USA.
5. Jones, T. A. (1985). Methods Enzymol. 115, 157-171.
6. Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.
7. Kuipers, O. P., Dijkman, R., Pals, C. E., Verheij, H. M. & de Haas, G. H. (1989). Protein Eng. 2, 467-471.
8. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
9. Luzzati, V. (1952). Acta Cryst. 5, 802-807.
10. Noel, J. P., Bingman, C. A., Deng, T., Dupureur, C. M., Hamilton, K. J., Jiang, R. T., Kwak, J. G., Sekharudu, C., Sundaralingam, M. & Tsai, M.-D. (1991). Biochemistry, 30, 11801-11811.
11. Scott, D. L., Otwinowski, Z., Gelb, M. H. & Sigler, P. B. (1990). Science, 250, 1563-1566.
12. Scott, D. L., White, S. P., Browning, J. L., Rosa, J. J., Gelb, M. H. & Sigler, P. B. (1991). Science, 254, 1007-1010.
13. Scott, D. L., White, S. P., Otwinowski, Z., Yuan, W., Gelb, M. H. & Sigler, P. B. (1990). Science, 250, 1541-1546.
14. Sekar, K., Sekharudu, C., Tsai, M.-D. & Sundaralingam, M. (1998). Acta Cryst. D54, 342-346.
15. Thunnissen, M. M. G. M., Eiso, A. B., Kalk, K. H., Drenth, J., Dijkstra, B. W., Kuipers, O. P., Dijkman, R., de Hass, G. H. & Verheij, H. M. (1990). Nature (London), 347, 689-691.
16. Tomoo, K., Ohishi, H., Ishida, T., Inoue, M., Ikeda, K., Sumiya, S. & Kitamura, K. (1994). Proteins, 19, 330-339.
17. White, S. P., Scott, D. L., Otwinowski, Z., Gelb, M. H. & Sigler, P. B. (1990). Science, 250, 1560-1563.
18. Yuan, W. & Gelb, M. H. (1988). J. Am. Chem. Soc. 110, 2665-2666.