Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin

Journal of Biological Chemistry

Volumn 274, Issue 33, 1999, Pages 23296-23304

  Nagpal, Sushma ^a   Gupta, Vibha ^a   Kaur, Kanwal J ^a   Salunke, Dinakar M ^a  

^a NATIONAL INSTITUTE OF IMMUNOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT; TRITRYPTICIN; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; ARTICLE; CIRCULAR DICHROISM; DRUG ACTIVITY; DRUG STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BONE MARROW; CIRCULAR DICHROISM; ESCHERICHIA COLI; MODELS, MOLECULAR; PEPTIDES; PROTEINS; SALMONELLA TYPHIMURIUM; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0033551685     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.33.23296     Document Type: Article

References (40)

1. Barra, D., Simmaco, M., and Boman, H. G. (1998) FEBS Lett. 430, 130-140
2. Hancock, R. E. W. (1997) Lancet 349, 418-422
3. Boman, H. G. (1995) Annu. Rev. Immunol. 13, 61-92
4. Nicolas, P., and Mor, A. (1995) Annu. Rev. Microbiol. 49, 277-304
5. Zanetti, M., Gennaro, R., and Romeo, D. (1995) FEBS Lett. 374, 1-5
6. Lichtenstein, A. K., Ganz, T., Nguyen, T.-M., Selsted, M. E., and Lehrer, R. I. (1988) J. Immunol. 140, 2686-2694
7. Levy, O., Weiss, J., Zarember, K., Ooi, C. E., and Elsbach, P. (1993) J. Biol. Chem. 268, 6058-6063
8. Zanetti, M., Del Sal, G., Storici, P., Schneider, C., and Romeo, D. (1993) J. Biol. Chem. 268, 522-526
9. Selsted, M. E., Novotny, M. J., Morris, W. L., Tang, Y.-Q., Smith, W., and Cullor, J. S. (1992) J. Biol. Chem. 267, 4292-4295
10. Storici, P., Sal, G. D., Schneider, C., and Zanetti, M. (1992) FEBS Lett. 314, 187-190
11. Pungercar, J., Strukelj, B., Kopitar, G., Renko, M., Lenarcic, B., and Turk, F. G. V. (1993) FEBS Lett. 336, 284-288
12. Lawyer, C., Pai, S., Watabe, M., Borgia, P., Mashimo, T., Eagleton, L., and Watabe, K. (1996) FEBS Lett. 390, 95-98
13. Hancock, R. E. W., and Lehrer, R. (1998) 16, 82-88
14. Gupta, H. M., Talwar, G. P., and Salunke, D. M. (1993) Proteins Struct. Funct. Genet. 16, 48-56
15. Lehrer, R. I., Rosenman, M., Harwig, S. S. S. L., Jachson, R., and Eisenhauer, P. (1991) J. Immunol. Methods 137, 167-173
16. Altschul, S. F., Gish, W., Miller, W., Myers, E. W., and Lipman, D. J. (1990) J. Mol. Biol. 215, 403-410
17. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Jr., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., and Tasumi, M. (1977) J. Mol. Biol. 112, 535-542
18. Weiner, S. J., Kollman, P. A., Nguyen, D. T., and Case, D. A. (1986) J. Comput. Chem. 7, 230-252
19. Woody, R. W. (1985) in Circular Dichroism of Peptides in Peptides: Anal. Synth. Biol. (Hruby, V. J., ed), Vol. 7, pp. 15-114, Academic Press, Inc., London
20. Boman, H. G., Marsh, J., and Goode, J. A. (1994) Antimicrobial Peptides, CIBA Foundation Symposium, Vol. 186, pp. 1-283, John Wiley & Sons, Inc., New York
21. Holak, T. A., Engstrom, A., Kraulis, P. J., Lindeberg, G., Bennich, H., Jones, A., Gronenborn, A. M., and Clore, G. M. (1988) Biochemistry 27, 7620-7629
22. Gazit, E., Miller, I. S., Biggin, P. C., Sansom, M. S. P., and Shai, Y. (1996) J. Mol. Biol. 258, 860-870
23. Terwilliger, T. C., and Eisenberg, D. (1982) J. Biol. Chem. 267, 6010-6015
24. Hill, C. P., Yee, J., Selsted, M. E., and Eisenberg, D. (1991) Science 251, 1481-1485
25. Skalicky, J. L., Selsted, M. E., and Pardi, A. (1994) Proteins Struct. Funct. Genet. 20, 52-67
26. Yao, J., Feher, V. A., Espejo, B. F., Reymond, M. T., Wright, P. E., and Dyson, H. J. (1994) J. Mol. Biol. 243, 736-753
27. Kaur, K. J., Khurana, S., and Salunke, D. M. (1997) J. Biol. Chem. 272, 5539-5543
28. Richardson, J. S. (1981) Adv. Protein Chem. 34, 167-339
29. Efimov, A. V. (1994) FEBS Lett. 355, 213-219
30. Rice, P. A., Goldman, A., and Steitz, T. A. (1990) Proteins Struct. Funct. Genet. 8, 334-340
31. Kobe, B., and Deisenhofer, J. (1993) Nature 366, 751-756
32. Chavali, G. B., Nagpal, S., Majumdar, S. S., Singh, O., and Salunke, D. M. (1997) J. Mol. Biol. 272, 731-740
33. Gupta, H. M., and Salunke, D. M. (1992) Curr. Sci. (Bangalore) 62, 374-376
34. Ludkte, S. J., He, K. Heller, W. T., Harroun, T. A., Yang, L., and Huang H. W. (1996) Biochemistry 35, 13723-13728
35. Falla, T. J., Karunaratne, D. N., and Hancock, R. E. W. (1996) J. Biol. Chem. 271, 19298-19303
36. Shai, Y. (1995) Trends Biochem. Sci. 20, 460-464
37. Casteels, P., and Tempst, P. (1994) Biochem. Biophys. Res. Commun. 199, 339-345
38. Skerlavaj, B., Romeo, D., and Gennaro, R. (1990) Infect. Immun. 58, 3724-3730
39. Boman, H. G., Agerberth, B., and Boman, A (1993) Infect. Immun. 61, 2978-2984
40. Yonezawa, A., Kuwahara, J., Fujii, N., and Sugiura, Y. (1992) Biochemistry 31, 2998-3004