Use of 1H NMR spectroscopy and computer simulations to analyze histidine pK(a) changes in a protein tyrosine phosphatase: Experimental and theoretical determination of electrostatic properties in a small protein

Biochemistry

Volumn 36, Issue 39, 1997, Pages 11984-11994

  Tishmack, Patrick A ^a   Bashford, Donald ^c   Harms, Etti ^b   Van Etten, Robert L ^a  

^a PURDUE UNIVERSITY   (United States)

^b PURDUE UNIVERSITY   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL PHOSPHATE; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; MUTANT PROTEIN; PROTEIN TYROSINE PHOSPHATASE;

ARTICLE; COMPUTER SIMULATION; CONTROLLED STUDY; ELECTRICITY; ENZYME KINETICS; MICHAELIS CONSTANT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PKA; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; ANIMAL; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; PH; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; CATTLE; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN-TYROSINE-PHOSPHATASE;

EID: 0030612614     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9712448     Document Type: Article

References (63)

1. Antosiewicz, J., McCammon, J. A., & Gilson, M. K. (1994) J. Mol. Biol. 238, 415-436.
2. Antosiewicz, J., McCammon, J. A., & Gilson, M. K. (1996) Biochemistry 35, 7819-7833.
3. Bashford, D., & Karplus, M. (1990) Biochemistry 29, 10219-10225.
4. Bashford, D., & Gerwert, K. (1992) J Mol. Biol. 224, 473-486.
5. Bashford, D., Case, D. A., Dalvit, C., Tennant, L., & Wright, P. E. (1993) Biochemistry 32, 8045-8056.
6. Beroza, P., Fredkin, D. R., Okamura, M. Y., & Feher, G. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 5804-5808.
7. Botelho, L. H., & Gurd, F. R. N. (1978) Biochemistry 17, 5188-5196.
8. Botelho, L. H., Friend, S. H., Matthew, J. B., Lehman, L. D., Hanania, G. I. H., & Gurd, F. R. N. (1978) Biochemistry 17, 5197-5205.
9. Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) J. Comput. Chem. 4, 187-217.
10. Brünger, A. T., & Karplus, M. (1988) Proteins: Struct., Funct., Genet. 4, 148-156.
11. Chiarugi, P., Cirri, P., Camici, G., Manao, G., Fiaschi, T., Raugei, G., Cappugi, G., & Ramponi, G. (1994) Biochem. J. 298, 427-433.
12. Davis, J. P., Zhou, M.-M., & Van Etten, R. L. (1994a) J. Biol. Chem. 269, 8734-8740.
13. Davis, J. P., Zhou, M.-M., & Van Etten, R. L. (1994b) Biochemistry 33, 1278-1286.
14. Evans, B., Tishmack, P. A., Pokalsky, C., Zhang, M., & Van Etten, R. L. (1996) Biochemistry 35, 13609-13617.
15. Gilson, M. K. (1995) Curr. Opin. Struct. Biol. 5, 216-223.
16. Glasoe, P. K., & Long, F. A. (1960) J. Am. Chem. Soc. 64, 188-190.
17. Honig, B., & Nicholls, A. (1995) Science 268, 1144-1149.
18. Kraulis, P. (1991) J. Appl. Crystallogr. 24, 946-950.
19. Lawrence, G. L., & Van Etten, R. L. (1981) Arch. Biochem. Biophys. 206, 122-131.
20. Levitt, M. H., Freeman, R., & Frenkiel, T. (1982) J. Magn. Reson. 47, 328-330.
21. Li, N. C., Tang, P., & Mathur, R. (1961) J. Am. Chem. Soc. 65, 1074-1076.
22. Li, Y., & Strohl, W. R. (1996) J. Bacteriol. 178, 136-142.
23. Linderstrøm-Lang, K. (1924) C. R. Lab. Carlsberg 15(7), 1-29.
24. Loewenthal, R., Sancho, J., & Fersht, A. R. (1992) J. Mol. Biol. 224, 759-770.
25. Loewenthal, R., Sancho, J., Reinikainen, T., & Fersht, A. R. (1993) J. Mol. Biol. 232, 574-583.
26. Logan, T. M., Shou, M.-M., Nettesheim, D. G., Meadows, R. P., Van Etten, R. L., & Fesik, S. W. (1994) Biochemistry 33, 11087-11096.
27. MacKerell, A. D., Jr., Bashford, D., Bellott, M., Dunbrack, R. L., Jr., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph, D., Kuchnir, L., Kuczera, K., Lau, F. T. K., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, P., Roux, B., Schlenkrich, M., Smith, J. C., Stote, R., Straub, J., Wiorkiewicz-Kuczera, J., & Karplus, M. (1992) FASEB J. 6, A143.
28. Markley, J. L. (1973) Biochemistry 12, 2245-2250.
29. Markley, J. L. (1975a) Acc. Chem. Res. 8, 70-80.
30. Markley, J. L. (1975b) Biochemistry 14, 3546-3554.
31. Markley, J. L. (1975c) Biochemistry 14, 3554-3561.
32. Markley, J. L., & Finkenstadt, W. R. (1975) Biochemistry 14, 3554-3561.
33. Matthew, J. B., & Gurd, F. R. N. (1986) Methods Enzymol. 130, 413-436.
34. Meadows, D. H. (1972) Methods Enzymol 26, 638-653.
35. Meadows, D. H., Markley, J. L., Cohen, J. S., Jardetsky, O. (1967) Proc. Natl. Acad. Sci. U.S.A. 58, 1307-1313.
36. Ostanin, K., Pokalsky, C., Wang, S., & Van Etten, R. L. (1995) J. Biol. Chem. 270, 18491-18499.
37. Ramette, R. W. (1981) Chemical Equilibrium and Analysis, p 361, Addison-Wesley Publishing Co., Reading, MA.
38. Ramponi, G. (1994) Adv. Protein Phosphatases 8, 1-25.
39. Reiher, W. E., III. (1985) Ph.D. Thesis, Harvard University.
40. Roberts, G. C. K., Meadows, D. H., & Jardetzky O. (1969) Biochemistry 8, 2053-2056.
41. Russell, A. J., Thomas, P. G., & Fersht, A. R. (1987) J. Mol. Biol. 193, 803-813.
42. Saini, M. S., Buchwald, S. L., Van Etten, R. L., & Knowles, J. R. (1981) J. Biol. Chem. 256, 10453-10455.
43. Sancho, J., Serrano, L., & Fersht, A. R. (1992) Biochemistry 31, 2253-2258.
44. Shimohama, S., Fujimoto, S., Taniguchi, T., & Kimura, J. (1994) Brain Res. 662, 185-188.
45. Shire, S. J., Hanania, G. I. H., & Gurd, R. N. (1974a) Biochemistry 13, 2967-2974.
46. Shire, S. J., Hanania, G. I. H., & Gurd, R. N. (1974b) Biochemistry 13, 2974-2979.
47. Su, X.-D., Taddei, N., Stefani, M., Ramponi, G., & Nordlund, P. (1994) Nature 370, 575-578.
48. Sudmeier, J. L., Evelhoch, J. L., &Jonsson, N. B.-H. (1980) J. Magn. Reson. 40, 377-390.
49. Tanford, C., & Kirkwood, J. G. (1957) J. Am. Chem. Soc. 79, 5333-5339.
50. Vandeyar, M. A., Weiner, M. P., Hutton, C. J., & Batt, C. A. (1988) Gene 65, 129-133.
51. Waheed, A., Laidler, P. M., Wo, Y.-Y. P., & Van Etten, R. L. (1988) Biochemistry 27, 4265-4273.
52. Warwicker, J., & Watson, H. C. (1982) J. Mol. Biol. 157, 671-679.
53. Wo, Y.-Y. P., Zhou, M.-M., Stevis, P., Davis, J. P., Zhang, Z.-Y., & Van Etten, R. L. (1992a) Biochemistry 31, 1712-1721.
54. Wo, Y.-Y. P., McCormack, A. L., Shabanowitz, J., Hunt, D. F., Davis, J. P., Mitchell, G. L., & Van Etten, R. L. (1992b) J. Biol. Chem. 267, 10856-10865.
55. Yang, Q., & Tonks, N. K. (1993) Adv. Protein Phosphatases 7, 359-372.
56. You, T., & Bashford, D. (1995) Biophys. J. 69, 1721-1733.
57. Zhang, M., Van Etten, R. L., & Stauffacher, R. L. (1994) Biochemistry 33, 11097-11105.
58. Zhang, M., Stauffacher, C. V., & Van Etten, R. L. (1995) Adv. Protein Phosphatases 9, 1-23.
59. Zhang, M., Zhou, M., Van Etten, R. L., & Stauffacher, C. V. (1997) Biochemistry 36, 15-23.
60. Zhang, Z.-Y., & Van Etten, R. L. (1990) Arch. Biochem. Biophys. 282, 39-49.
61. Zhang, Z.-Y., & Dixon, J. E. (1994) Adv. Enzymol Relat.Areas Mol. Biol.68, 1-36.
62. Zhang, Z., Harms, E., & Van Etten, R. L. (1994) J. Biol. Chem. 269, 25947-25950.
63. Zhou, M.-M., Davis, J. P., & Van Etten, R. L. (1993) Biochemistry 32, 8479-8486.