Solution structure and dynamics of the plasminogen kringle 2-AMCHA complex: 31-helix in homologous domains

Biochemistry

Volumn 38, Issue 48, 1999, Pages 15741-15755

  Marti, Daniel N ^a   Schaller, Johann ^b   Llinás, Miguel ^a  

^a CARNEGIE MELLON UNIVERSITY   (United States)

^b UNIVERSITY OF BERN   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINOVALERIC ACID; AMINOCAPROIC ACID; ANTIFIBRINOLYTIC AGENT; ARGININE; ASPARTIC ACID; GLUTAMINE; GUANIDINE; HYDROXIDE; LEUCINE; LYSINE; PHENYLALANINE; PLASMINOGEN; TRANEXAMIC ACID; TRYPTOPHAN; TYROSINE;

ARTICLE; CONTROLLED STUDY; DRUG PROTEIN BINDING; ESCHERICHIA COLI; KRINGLE DOMAIN; LIGAND BINDING; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANTIFIBRINOLYTIC AGENTS; BINDING SITES; CIRCULAR DICHROISM; HYDROGEN BONDING; KRINGLES; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PLASMINOGEN; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; TRANEXAMIC ACID;

EID: 0033619701     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9917378     Document Type: Article

References (97)

1. Lucas, M. A., Fretto, L. J., and McKee, P. A. (1983) J. Biol. Chem. 258, 4249-4256.
2. Wimann, B., Lijnen, H. R., and Collen, D. (1979) Biochim. Biophys. Acta 579, 142-154.
3. Lijnen, H. R., Hoylaerts, M., and Collen, D. (1980) J. Biol. Chem. 255, 10214-10222.
4. Silverstein, R. L., Leung, L. L. K., Harpel, P. C., and Nachman, R. L. (1984) J. Clin. Invent. 74, 1625-1633.
5. Ponting, C. P., Marshall, J. M., and Cederholm-Williams, S. A. (1992) Blood Coagulation Fibrinolysis 3, 605-614.
6. Miles, L. A., and Plow, E. F. (1985) J. Biol. Chem. 260, 4303-4311.
7. Hajjar, K. A., Harpel, P. C., Jaffe, E. A., and Nachman, R. L. (1986) J. Biol. Chem. 261, 11656-11662.
8. Cao, Y., Ji, R. W., Davidson, D., Schaller, J., Marti, D., Söhndel, S., McCance, S. G., O'Reilly, M. S., Llinás, M., and Folkman, J. (1996) J. Biol. Chem. 271, 29461-29467.
9. Cao, Y., Chen, A., An, S. S. A., Ji, R.-W., Davidson, D., Cao, Y., and Llinás, M. (1997) J. Biol. Chem. 272, 22924-22928.
10. Ji, W. R., Barrientos, L. G., Llinás, M., Gray, H., Villareal, X., DeFord, M. E., Castellino, F. J., Kramer, R. A., and Trail, P. A. (1998) Biochem. Biophys. Res. Commun. 247, 414-419.
11. Ji, W. R., Castellino, F. J., Chang, Y., DeFord, M. E., Gray, H., Villarreal, X., Kodri, M. E., Marti, D. N., Llinás, M., Schaller, J., Kramer, R. A., and Trail, P. A. (1998) FASEB J. 15, 1731-1738.
12. Llinás, M., De Marco, A., Hochschwender, S. M., and Laursen, R. A. (1983) Eur. J. Biochem. 135, 379-391.
13. Tulinsky, A., Park, C. H., and Skrypczak-Jankun, E. (1988) J. Mol. Biol. 202, 885-901.
14. Byeon, I.-J. L., and Llinás, M. (1991) J. Mol. Biol. 222, 1035-1051.
15. Wu, T.-P., Padmanabhan, K., Tulinsky, A., and Mulichak, A. M. (1991) Biochemistry 30, 10589-10594.
16. Rejante, M. R., and Llinás, M. (1994) Eur. J. Biochem. 221, 939-949.
17. Mathews, I. I., Vanderhoff-Hanaver, P., Castellino, F. J., and Tulinsky, A. (1996) Biochemistry 35, 2567-2576.
18. Mikol, V., LoGrasso, P. V., and Boettcher, B. R. (1996) J. Mol. Biol. 256, 751-761.
19. Motta, A., Laursen, R. A., Llinás, M., Tulinsky, A., and Park, C. H. (1987) Biochemistry 26, 3827-3836.
20. Thewes, T., Constantine, K., Byeon, I.-J. L., and Llinás, M. (1990) J. Biol. Chem. 265, 3906-3915.
21. Rejante, M. R., Byeon, I.-J. L., and Llinás, M. (1991) Biochemistry 30, 11081-11092.
22. Menhart, N., Sehl, L. C., Kelley, R. F., and Castellino, F. J. (1991) Biochemistry 30, 1948-1957.
23. Hoover, G. J., Menhart, N., Martin, A., Warder, S., and Castellino, F. J. (1993) Biochemistry 32, 10936-10943.
24. Nielsen, P. R., Einer-Jensen, K., Holtet, T. L., Andersen, B. D., Poulsen, F. M., and Thørgersen, H. C. (1993) Biochemistry 32, 13019-13025.
25. McCance, S. G., Menhart, N., and Castellino, F. J. (1994) J. Biol. Chem. 269, 32405-32410.
26. Marti, D., Schaller, J., Ochensberger, B., and Rickli, E. E. (1994) Eur. J. Biochem. 219, 455-462.
27. Söhndel, S., Hu, C.-K., Marti, D., Affolter, M., Schaller, J., Llinás, M., and Rickli, E. E. (1996) Biochemistry 35, 2357-2364.
28. An, S. S. A., Marti, D. N., Carreño, C., Albericio, F., Schaller, J., and Llinás, M. (1998) Protein Sci. 7, 1947-1959.
29. An, S. S. A., Carreño, C., Marti, D. N., Schaller, J., Albericio, F., and Llinás, M. (1998) Protein Sci. 7, 1960-1969.
30. Marti, D., Hu, C.-K., An, S. S. A., von Haller, P., Schaller, J., and Lliná;s, M. (1997) Biochemistry 36, 11591-11604.
31. Muchmore, D. C., McIntosh, L. P., Russell, C. B., Anderson, D. E., and Dahlquist, F. W. (1989) Methods Enzymol. 177, 44-73.
32. Johnson, W. C. (1999) Proteins 35, 307-312.
33. Aue, W. P., Bartholdi, E., and Ernst, R. R. (1976) J. Chem. Phys. 64, 2229-2246.
34. Piantini, U., Sørensen, O. W., and Ernst, R. R. (1982) J. Am. Chem. Soc. 104, 6800-6801.
35. Bax, A., and Davis, D. G. (1985) J. Magn. Reson. 65, 355-360.
36. Jeener, J., Meier, B. H., Bachmann, P., and Ernst, R. R. (1979) J. Chem. Phys. 71, 4546-4553.
37. Sklenar, V., Piotto, M., Leppik, R., and Saudek, V. (1993) J. Magn. Reson., Ser. A 102, 241-245.
38. Mori, S., Abeygunawardana, C., Johnson, M. O., and van Zijl, P. C. M. (1995) J. Magn. Reson., Ser. B 108, 94-98.
39. States, D. J., Haberkorn, R. A., and Ruben, D. J. (1982) J. Magn. Reson. 48, 286-292.
40. Zuiderweg, E. R. P., and Fesik, S. W. (1989) Biochemistry 28, 2387-2391.
41. Marion, D., Kay, L. E., Sparks, S. W., Torchia, D. A., and Bax, A. (1989) J. Am. Chem. Soc. 111, 1515-1517.
42. Marion, D., Driscoll, P. C., Kay, L. E., Wingfield, P. T., Bax, A., Gronenborn, A. M., and Clore, G. M. (1989) Biochemistry 28, 6150-6156.
43. Schleucher, J., Sattler, M., and Griesinger, C. (1993) Angew. Chem., Int. Ed. 32, 1489-1491.
44. Vuister, G. W., and Bax, A. (1993) J. Am. Chem. Soc. 115, 7772-7777.
45. Archer, S. J., Ikura, M., Torchia, D. A., and Bax, A. (1991) J. Magn. Reson. 95, 636-641.
46. Düx, P., Whitehead, B., Boelens, R., Kaptein, R., and Vuister, G. W. (1997) J. Biomol. NMR 10, 301-306.
47. Kay, L. E., Ikura, M., Tschudin, R., and Bax, A. (1990) J. Magn. Reson. 89, 496-414.
48. Grzesiek, S., and Bax, A. (1992) J. Magn. Reson. 96, 432-440.
49. Bax, A., and Ikura, M. (1991) J. Biomol. NMR 1, 99-104.
50. Montelione, G. T., Lyons, B. A., Emerson, S. D., and Tashiro, M. (1992) J. Am. Chem. Soc. 114, 10974-10975.
51. Grzesiek, S., Anglister, J., and Bax, A. (1993) J. Magn. Reson., Ser. B 101, 114-119.
52. Carlomagno, T., Maurer, M., Sattler, M., Schwendinger, M. G., Glaser, S. J., and Griesinger, C. (1996) J. Biomol. NMR 8, 161-170.
53. Shaka, A. J., Lee, C. J., and Pines, A. (1988) J. Magn. Reson. 77, 274-293.
54. Shaka, A. J., Keeler, J., Frenkiel, T., and Freeman, R. (1983) J. Magn. Reson. 52, 335-338.
55. De Marco, A. (1977) J. Magn. Reson. 26, 527-528.
56. Live, D. H., Davis, D. G., Agosta, W. C., and Cowburn, D. (1984) J. Am. Chem. Soc. 106, 1939-1943.
57. De Marco, A., Llinás, M., and Wüthrich, K. (1978) Biopolymers 17, 617-636.
58. Pardi, A., Billeter, M., and Wüthrich, K. (1984) J. Mol. Biol. 180, 741-751.
59. Brünger, A. T. (1992) X-PLOR 3.1 User Manual, Yale University Press, New Haven, CT.
60. Nilges, M., Kuszewsky, J., and Brünger, A. T. (1991) in Computational Aspects of the Study of Biological Macromolecules by NMR (Hoch, J. C., Ed.) Plenum Press, New York.
61. Kuszewsky, J., Nilges, M., and Brünger, A. T. (1992) J. Biomol. NMR 2, 33-56.
62. Laskowsky, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
63. Koradi, R., Billeter, M., and Wüthrich, K. (1996) J. Mol. Graphics 14, 51-55.
64. King, S. M., and Johnson, W. C. (1999) Proteins 35, 307-312.
65. Dayie, K. T., and Wagner, G. (1994) J. Magn. Reson., Ser. A 111, 121-126.
66. Lipari, G., and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546-4559.
67. Lipari, G., and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4559-4570.
68. Palmer, A. G., Rance, M., and Wright, P. E. (1991) J. Am. Chem. Soc. 113, 4371-4380.
69. Venyaminov, S. Y., and Yang, J. T. (1996) in Circular dichroism and the conformational analysis of biomolecules (Fasman, G. D., Ed.) pp 69-107, Plenum Press, New York.
70. De Marco, A., Pluck, N. D., Bányai, L., Trexler, M., Laursen, R. A., Patthy, L., Llinás, M., and Williams, R. J. P. (1985) Biochemistry 24, 748-753.
71. Li, X., Bokman, A. M., Llinás, M., Smith, R. A. G., and Dobson, C. M. (1994) J. Mol. Biol. 235, 1548-1559.
72. Chang, Y., Mochalkin, I., McCance, S. G., Cheng, B., Tulinsky, A., and Castellino, F. J. (1998) Biochemistry 37, 3258-3271.
73. Wishart, D. S., Skyes, B. D., and Richards, F. M. (1991) J. Mol. Biol. 222, 311-333.
74. Adzhubei, A. A., and Sternberg, M. J. E. (1993) J. Mol. Biol. 229, 472-493.
75. Sreerama, N., and Woody, R. W. (1994) Biochemistry 33, 10022-10025.
76. Wüthrich, K. (1986) NMR of proteins and nucleic acids, John Wiley and Sons, New York.
77. Mulichak, A. M., Tulinsky, A., and Ravichandran, K. G. (1991) Biochemistry 30, 10576-10588.
78. de Vos, A. M., Ultsch, M. H., Kelley, R. F., Padmanabhan, K., Tulinsky, A., Westbrook, M. L., and Kossiakoff, A. A. (1992) Biochemistry 31, 270-279.
79. Ramesh, V., Gyenes, M., Patthy, L., and Llinás, M. (1986) Eur. J. Biochem. 159, 581-595.
80. Roseman, M. A. (1988) J. Mol. Biol. 200, 513-522.
81. Tulinsky, A., Park, C. H., Mao, B., and Llinás M. (1988) Proteins: Struct., Funct., Genet. 3, 85-96.
82. Trexler, M., Váli, Z., and Patthy, L. (1982) J. Biol. Chem. 257, 7401-7406.
83. Chang, Y., Zajicek, J., and Castellino, F. J. (1997) Biochemistry 36, 7652-7663.
84. Rejante, M. R. (1992) Ph.D. Dissertation, Carnegie Mellon University, Pittsburgh, PA.
85. De Marco, A., Petros, A. M., Laursen, R. A., and Llinás, M. (1987) Eur. Biophys. J. 14, 359-368.
86. Byeon, I.-J. L., Kelley, R. F., Mulkerrin, M. G., An, S. S. A., and Llinás, M. (1995) Biochemistry 34, 2739-2750.
87. Cox, M., Schaller, J., Boelens, R., Kaptein, R., Rickli, E., and Llinás, M. (1994) Chem. Phys. Lipids 67/68, 43-58.
88. Ramesh, V., Petros, A. M., Llinás, M., Tulinsky, A., and Park, C. H. (1987) J. Mol. Biol. 198, 481-498.
89. King, S. M., and Johnson, W. C. (1999) Proteins 35, 313-320.
90. Castellino, F. J., de Serrano, V. S., Powell, J. R., Johnson, W. R., and Beals, J. M. (1986) Arch. Biochem. Biophys. 247, 312-320.
91. Cleary, S., Mulkerrin, M. G., and Kelley, R. F. (1989) Biochemistry 28, 1884-1891.
92. Wu, T.-P., Padmanabhan, K., and Tulinsky, A. (1994) Blood Coagulation Fibrinolysis 5, 157-166.
93. Mochalkin, I., Cheng, B., Klezovitch, O., Scanu, A. M., and Tulinsky, A. (1999) Biochemistry 38, 1990-1998.
94. Ultsch, M., Lokker, N. A., Godowski, P. J., and de Vos, A. M. (1998) Structure 6, 1383-1393.
95. Seshadri, T. P., Tulinsky, A., Skrzypczak-Jankun, E., and Park, C. H. (1991) J. Mol. Biol. 220, 481-494.
96. Ami, R. K., Padmanabhan, K., Padmanabhan, K. P., Wu, T.-P., and Tulinsky, A. (1993) Biochemistry 32, 4727-4737.
97. Affolter, M., Schaller, J., and Rickli, E. E. (1993) Protein Sequences Data Anal. 5, 207-211.