Molecular model of interleukin 12 that highlights amino acid sequence homologies with adhesion domains and gastrointestinal peptides

Journal of Molecular Graphics

Volumn 14, Issue 3, 1996, Pages 148-157

  Dwyer, Donard S ^a  

^a LOUISIANA STATE UNIV MEDICAL CENTER   (United States)

Author keywords

Adhesion sequences; Gastrointestinal peptides; Interleukin 12; Molecular modeling

Indexed keywords

CD4 ANTIGEN; CYTOKINE RECEPTOR; FIBRONECTIN; GASTROINTESTINAL POLYPEPTIDE; GLUCAGON; GROWTH HORMONE RECEPTOR; INTERLEUKIN 12; PROPERDIN; PROTEIN SUBUNIT; SECRETIN; THROMBOSPONDIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANTIGENS, CD4; CELL ADHESION MOLECULES; EPITOPES; FIBRONECTINS; GLUCAGON; INTERLEUKIN-12; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; RECEPTORS, CYTOKINE; RECEPTORS, SOMATOTROPIN; SECRETIN; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0030175254     PISSN: 02637855     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0263-7855(96)00044-6     Document Type: Article

References (55)

1. 1 Kobayashi, M., Fitz, L., Ryan, M., Hewick, R.M., Clark, S.C., Chan, S., Loudon, R., Sherman, F., Perussia, B., and Trinchieri, G. Identification and purification of natural killer cell stimulatory factor (NKSF), a cytokine with multiple biologic effects of human lymphocytes. J. Exp. Med. 1989, 170, 827-845
2. 2 Stern, A.S., Podlaski, F.J., Hulmes, J.D., Pan, Y.-C.E., Quinn, P.M., Wolitzky, A.G., Familletti, P.C., Stremlo, D.L., Truitt, T., Chizzonite, R., and Gately, M.K. Purification to homogeneity and partial characterization of cytotoxic lymphocyte maturation factor from human B-lymphoblastoid cells. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 6808-6812
3. 3 Trinchieri, G. Interleukin-12: A proinflammatory cytokine with immunoregulatory functions that bridge innate resistance and antigen-specific adaptive immunity. Annu. Rev. Immunol. 1995, 13, 251-276
4. 4 Clerici, M., Lucey, D.R., Berzofsky, J.A., Pinto, L.A., Wynn, T.A., Blatt, S.P., Dolan, M.J., Hendrix, C.W., Wolf, S.F., and Shearer, G.M. Restoration of HIV-specific cell-mediated immune responses by interleukin-12 in vitro. Science 1993, 262, 1721-1724
5. 5 Heinzel, F.P., Schoenhaut, D.S., Rerko, R.M., Rosser, L.E., and Gately, M.K. Recombinant interleukin 12 cures mice infected with Leishmania major. J. Exp. Med. 1993, 177, 1505-1509
6. 6 Sypek, J.P., Chung, C.L., Mayor, S.E., Subramanyam, J.M., Goldman, S.J., Sieburth, D.S., Wolf, S.F., and Schaub, R.G. Resolution of cutaneous leishmaniasis: Interleukin 12 initiates a protective T helper type 1 immune response. J. Exp. Med. 1993, 177, 1797-1802
7. 7 Gazzinelli, R.T., Hieny, S., Wynn, T.A., Wolf, S., and Sher, A. Interleukin 12 is required for the T-lymphocyte-independent induction of Interferon γ by an intracellular parasite and induces resistance in T-cell-deficient hosts. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 6115-6119
8. 8 Stevenson, M.M., Tam, M.F., Wolf, S.F., and Sher, A. IL-12-induced protection against blood-stage Plasmodium chabaudi AS requires IFN-γ and TNF-α and occurs via a nitric oxide-dependent mechanism. J. Immunol 1995, 155, 2545-2556
9. 9 Brunda, M.J., Luistro, L., Warrier, R.R., Wright, R.B., Hubbard, B.R., Murphy, M., Wolf, S.F., and Gately, M.K. Antitumor and antimetastatic activity of interleukin 12 against murine tumors. J. Exp. Med. 1993, 178, 1223-1230
10. 10 D'Andrea, A., Rengaraju, M., Valiante, N.M., Chehimi, J., Kubin, M., Aste, M., Chan, S.H., Kobayashi, M., Young, D., Nickbarg, E., Chizzonite, R., Wolf, S.F., and Trinchieri, G. Production of natural killer cell stimulatory factor (interleukin 12) by peripheral blood mononuclear cells. J. Exp. Med. 1991, 176, 1387-1398
11. 11 Wolf, S.F., Temple, P.A., Kobayashi, M., Young, D., Dicig, M., Lowe, L., Dzialo, R., Fitz, L., Ferenz, C., Hewick, R.M., Kelleher, K., Herrmann, S. H., Clark, S.C., Azzoni, L., Chan, S.H., Trinchieri, G., and Perussia, B. Cloning of cDNA for natural killer cell stimulatory factor, a heterodimeric cytokine with multiple biologic effects on T and natural killer cells. J. Immunol 1991, 146, 3074-3081
12. 12 Gubler, U., Chua, A.O., Schoenhaut, D.S., Dwyer, C.M., McComas, W., Motyka, R., Nabavi, N., Wolitzky, A.G., Quinn, P.M., Familletti, P.C., and Gately, M.K. Coexpression of two distinct genes is required to generate secreted bioactive cytotoxic lymphocyte maturation factor. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 4143-4147
13. 13 Merberg, D.M., Wolf, S.F., and Clark, S.C. Sequence similarity between NKSF and the IL-6/G-CSF family. Immunol. Today 1992, 13, 77-78
14. 14 Gearing, D.P., and Cosman, D. Homology of the p40 subunit of natural killer cell stimulatory factor (NKSF) with the extracellular domain of the interleukin-6 receptor. Cell 1991, 66, 9-10
15. 15 Bazan, J.F. A novel family of growth factor receptors: A common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and the p75 IL-2 receptor β chain. Biochem. Biophys. Res. Commun. 1989, 164, 788-795
16. 16 Cosman, D., Lyman, S.D., Idzerda, R.L., Beckmann, M.P., Park, L.S., Goodwin, R.G., and March, C.J. A new cytokine receptor superfamily. Trends Biochem. Sci. 1990, 15, 265-270
17. 17 Dayhoff, M.O., Schwartz, R.M., and Orcutt, B.C. Establishing homologies in protein sequences. Methods Enzymol. 1983, 91, 524-545
18. 18 Chou, P.Y. and Fasman, G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol 1978, 47, 45-148
19. 19 Garnier, J., and Robson, B. The GOR method for predicting secondary structures in proteins. In: Prediction of Protein Structure and the Principles of Protein Conformation. (Fasman, G.D., ed.). Plenum Press, New York, 1989, pp. 417-465
20. 20 Bernstein, F.C., Koetzle, T.F., Williams, J.B., Meyer, E.F. Jr., Brice, M.D., Rodgers, J.R., Kennard, O., Shimanouchi, T., and Tasumi, M. The Protein Data Bank: A computer-based archival file for macromolecular structures. J. Mol. Biol. 1977, 112, 535-542
21. 21 Abola, E.E., Bernstein, F.C., Bryant, S.H., Koetzle, T.F., and Weng, J. Protein Data Bank. In: Crystallographic Databases: Information Content, Software Systems, Scientific Applications. (Allen, F.H., Bergerhoff, G., and Sievers, R., eds.). Data Commission of the International Union of Crystallography, Bonn, 1987, pp. 107-132
22. 22 de Vos, A.M., Ultsch, M., and Kossiakoff, A.A. Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science 1992, 255, 306-312
23. 23 Wang, J., Yan, Y., Garrett, T.P., Liu, J., Rodgers, D.W., Garlick, R.L., Tarr, G.E., Husain, Y., Reinherz, E.L., and Harrison, S.C. Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature (London) 1990, 348, 411-418
24. 24 Tangarone, B.S., Vath, J.E., Nickbarg, E.B., Yu, W., Harris, A.S., and Scoble, H.A. The disulfide bond structure of recombinant human interleukin-12. (Abstract.) In: Ninth Symposium of the Protein Society, 1995, pp. 00-00
25. 25 Ling, P., Chizzonite, R., and Hakimi J. Epitope mapping of inhibitory anti-human IL-12 antibodies by homolog-scanning mutagenesis. (Abstract.) In: Ninth International Congress of Immunology, 1995, p. 302.
26. 26 Sasaki, M., Kleinman, H.K., Huber, H., Deutzmann, R., and Yamada, Y. Laminin, a multidomain protein: The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains. J. Biol. Chem. 1988, 263, 16536-16544
27. 27 Tomasini, B.R., and Mosher, D.F. Vitronectin. Prog. Hemostasis Thromb. 1991, 10, 269-305
28. 28 de Bruijn, M.H., and Fey, G.H. Human complement component C3: cDNA coding sequence and derived primary structure. Proc. Natl. Acad. Sci. U.S.A. 1985, 82, 708-712
29. 29 Schwarzbauer, J.E., Tamkun, J.W., Lemischka, I.R., and Hynes, R.O. Three different fibronectin mRNAs arise by alternative splicing within the coding region. Cell 1983, 35, 421-431
30. 30 Schoenhaut, D.S., Chua, A.O., Wolitzky, A.G., Quinn, P.M., Dwyer, C.M., McComas, W., Familletti, P.C., Gately, M.K., and Gubler, U. Cloning and expression of murine IL-12. J. Immunol. 1992, 148, 3433-3340
31. 31 Plow, E.F., Srouji, A.H., Meyer, D., Marguerie, G., and Ginsberg, M.H. Evidence that three adhesive proteins interact with a common recognition site on activated platelets. J. Biol. Chem. 1984, 259, 5388-5391
32. 32 Goundis, D., and Reid, K.B. Properdin, the terminal complement components, thrombospondin and the circumsporozoite protein of malaria parasites contain similar sequence motifs. Nature (London) 1988, 335, 82-85
33. 33 Robson, K.J., Hall, J.R., Jennings, M.W., Harris, T.J., Marsh, K., Newbold, C.I., Tate, V.E., and Weatherall, D.J. A highly conserved amino-acid sequence in thrombospondin, properdin and in proteins from sporozoites from blood stages of a human malaria parasite. Nature (London) 1988, 335, 79-82
34. 34 Jörnvall, H., Carlström, A., Pettersson, T., Jacobsson, B., Persson, M., and Mutt, V. Structural homologies between prealbumin, gastrointestinal prohormones and other proteins. Nature (London) 1981, 291, 261-263
35. 35 Tatemoto, K. Neuropeptide Y: Complete amino acid sequence of the brain peptide. Proc. Natl. Acad. Sci. U.S.A. 1982, 79, 5485-5489
36. 36 Ruoslahti, E., and Pierschbacher, M.D. New perspectives in cell adhesion: RGD and integrins. Science 1987, 238, 491-497
37. 37 Patthy, L. Homology of a domain of the growth hormone/prolactin receptor family with type III modules of fibronectin. Cell 1990, 61, 13-14
38. 38 Yamada, K.M. Adhesive recognition sequences. J. Biol. Chem. 1991, 266, 12809-12812
39. 39 Kopin, A.S., Wheeler, M.B., and Leiter, A.B. The secretin gene: Evolutionary history, alternative splicing, and developmental regulation. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 2299-2303
40. 40 Bell, G.I., Sanchez-Pescador, R., Laybourn, P.J., and Najarian, R.C. Exon duplication and divergence in the human preproglucagon gene. Nature (London) 1983, 304, 368-371
41. 41 Wrighton, N., Campbell, L.A., Harada, N., Miyajima, A., and Lee, F. The murine interleukin-4 receptor gene: Genomic structure, expression and potential for alternative splicing. Growth Factors 1992, 6, 103-118
42. 42 Shibuya, H., Yoneyama, M., Nakamura, Y., Harada, H., Hatakeyama, M., Minamoto, S., Kono, T., Doi, T., White, R., and Taniguchi, T. The human interleukin-2 receptor β chain gene: Genomic organization, promoter analysis and chromosomal assignment. Nucleic Acids Res. 1990, 18, 3697-3703
43. 43 Godowski, P.J., Leung, D.W., Meacham, L.R., Galgani, J.P., Hellmiss, R., Keret, R., Rotwein, P.S., Parks, J.S., Laron, Z., and Wood, W.I. Characterization of the human growth hormone receptor gene and demonstration of a partial gene deletion in two patients with Laron-type dwarfism. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 8083-8087
44. 44 Withka, J.M., Wyss, D.F., Wagner, G., Arulanandam, A.R., Reinherz, E.L., and Recny, M.A. Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2. Structure 1993, 1, 69-81
45. 45 Walter, M.R., Windsor, W.T., Nagabhushan, T.L., Lundell, D.J., Lunn, C.A., Zauodny, P.J., and Narula, S.K. Crystal structure of a soluble complex between interferon-γ and its soluble high-affinity receptor. Nature (London) 1995, 376, 230-235
46. 46 Doolittle, R.F. Redundancies in protein sequences. In: Prediction of Protein Structure and the Principles of Protein Conformation. (Fasman, G.D., ed.). Plenum Press, New York, 1989, pp. 599-623
47. 47 Bazan, J.F, Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 6934-6938
48. 48 Adelson, J.W. Enterosecretory proteins. Nature (London) 1971, 229, 321-325
49. 4)β1-1Cer] and has a sequence homology with other proteins that bind sulfated glycoconjugates. J. Biol. Chem. 1990, 265, 2852-2855
50. 50 Tuszynski, G.P., Gasic, T.B., Rothman, V.L., Knudsen, K.A., and Gasic, G.J. Thrombospondin, a potentiator of tumor cell metastasis. Cancer Res. 1987, 47, 4130-4133
51. 51 Humphries, M.J., Olden, K., and Yamada, K.M. A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells. Science 1986, 233, 467-470
52. 52 Gehlsen, K.R., Argraves, W.S., Pierschbacher, M.D., and Ruoslahti, E. Inhibition of in vitro tumor cell invasion by Arg-Gly-Asp-containing synthetic peptides. J. Cell Biol. 1988, 106, 925-930
53. 53 Rola-Pleszczynski, M., Bolduc, D., and St.-Pierre, S. The effects of vasoactive intestinal peptide on human natural killer cell function. J. Immunol. 1985, 135, 2569-2573
54. 54 Stanisz, A.M., Befus, D., and Bienenstock, J. Differential effects of vasoactive intestinal peptide, substance P and somatostatin on immunoglobulin synthesis and proliferations by lymphoctyes from Peyer's patches, mesenteric lymph nodes, and spleen. J. Immunol. 1986, 136, 152-156
55. 55 Dwyer, D.S. Interleukin-12 displays segmental homology with cell adhesion sequences in thrombospondin and circumsporozote proteins and with gastrointestinal peptides. (Abstract.) In: Ninth International Congress of Immunology. 1995, p. 298