High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37β: Structural basis for a high-affinity T-state

Biochemistry

Volumn 37, Issue 13, 1998, Pages 4358-4373

  Kavanaugh, Jeffrey S ^a   Weydert, Jamie A ^a   Rogers, Paul H ^a   Arnone, Arthur ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARAGINE; ASPARTIC ACID; BETA GLOBIN; DIMER; DIPEPTIDE; GLUTAMINE; GLYCINE; HEMOGLOBIN; PROLINE; RECOMBINANT PROTEIN; TETRAMER; TRYPTOPHAN; TYROSINE;

ARTICLE; CHEMICAL BOND; CRYSTAL STRUCTURE; MUTATION; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STEREOCHEMISTRY; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

AMINO ACID SUBSTITUTION; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HEMOGLOBIN A; HUMANS; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; REPRODUCIBILITY OF RESULTS; TRYPTOPHAN;

EID: 0032584278     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9708702     Document Type: Article

References (46)

1. Mills, F. C., Johnson, M. L., and Ackers, G. K. (1976) Biochemistry 15, 5350-5362.
2. Perutz, M. F. (1970) Nature 228, 726-734.
3. Baldwin, J. M., and Chothia, C. (1979) J. Mol. Biol. 129, 175-220.
4. Perutz, M. F. (1989) Q. Rev. Biophys. 22, 139-236.
5. Turner, G. J., Galacteros, F., Doyle, M. L., Hedlund, B., Pettigrew, D. W., Turner, B. W., Smith, F. R., Moo-Penn, W., Rucknagel, D. L., and Ackers, G. K. (1992) Proteins 14, 333-350.
6. Kavanaugh, J. S., Chafin, D. R., Arnone, A., Mozzarelli, A., Rivetti, C., Rossi, G. L., Kwiatkowski, L. D., and Noble, R. W. (1995) J. Mol. Biol. 248, 136-150.
7. Sasaki, J., Imamura, T., and Yanase, T. (1978) J. Biol. Chem. 253, 87-94.
8. Sharma, V. S., Newton, G. L., Ranney, H. M., Ahmed, F., Harris, J. W., and Danish, E. H. (1980) J. Mol. Biol. 144, 267-280.
9. Ishimori, K., Imai, K., Miyazaki, G., Kitagawa, T., Wada, Y., Morimoto, H., and Morishima, I. (1992) Biochemistry 31, 3256-3264.
10. Owen, M. C., Ockelford, P. A., and Wells, R. M. (1993) Hemoglobin 17, 513-521.
11. Britain, T. (1994) Biochem. J. 300, 553-556.
12. Vallone, B., Bellelli, A., Miele, A. E., Brunori, M., and Fermi, G. (1996) J. Biol. Chem. 271, 12472-12480.
13. Kiger, L., Klinger, A. L., Kwiatkowski, L. D., De Young, A., Doyle, M. L., Holt, J. M., Noble, R. W., and Ackers, G. K. (1999) Biochemistry 37, 4336-4345.
14. Kwiatkowski, L. D., Hui, H. L., Wierzba, A., Noble, R. W., Walder, R. Y., Peterson, E. S., Sligar, S. G., and Sanders, K. E. (1998) Biochemistry 37, 4325-4335.
15. Peterson, E. S., and Friedman, J. M. (1998) Biochemistry 37, 4346-4357.
16. Hernan, R. A., Hui, H. L, Andracki, M. E., Noble, R. W., Sligar, S. G., Walder, J. A., and Walder, R. Y. (1992) Biochemistry 31, 8619-8628.
17. Doyle, M. L., Lew, G., De Young, A., Kwiatkowski, L., Wierzba, A., Noble, R. W., and Ackers, G. K. (1992) Biochemistry 31, 8629-8639.
18. Kavanaugh, J. S., Rogers, P. H., and Arnone, A. (1992) Biochemistry 31, 8640-8647.
19. Riggs, A. (1981) Methods Enzymol. 76, 5-29.
20. Ward, K. B., Wishner, B. C., Lattman, E. E., and Love, W. E. (1975) J. Mol. Biol. 98, 161-177.
21. Arnone, A., Rogers, P. H., and Briley, P. D. (1980) in Biophysics and Physiology of Carbon Dioxide (Bauer, C., Gros, G., and Bartels, H., Eds.) pp 67-74, Springer-Verlag, Berlin.
22. Metzler, C. M., Rogers, P. H., Arnone, A., Martin, D. S., and Metzler, D. E. (1979) Methods Enzymol. 62, 551-558.
23. Greer, J. (1971) J. Mol. Biol. 59, 107-126.
24. Fitzgerald, P. M. D., and Love, W. E. (1979) J. Mol. Biol. 132, 603-619.
25. Perutz, M. F. (1968) J. Crystal Growth 2, 54-56.
26. Howard, A. J., Nielson, C., and Xuong, N. H. (1985) Methods Enzymol. 114, 452-472.
27. Brünger, A. T. (1992) Nature 355, 472-474.
28. Kavanaugh, J. S., Rogers, P. H., Case, D. A., and Arnone, A. (1992) Biochemistry 31, 4111-4121.
29. Hendrickson, W. A. (1985) Methods Enzymol. 115, 252-270.
30. Sheriff, S. (1987) J. Appl. Crystallogr. 20, 53-55.
31. Cambillau, C. (1989) in Silicon Graphics Geometry Partners Directory, spring vol. p 61, Silicon Graphics, Mountain View, CA.
32. Jones, T. A. (1985) Methods Enzymol. 115, 157-189.
33. Brünger, A. T. (1992) XPLOR, Version 3.1, Yale University Press, New Haven and London.
34. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
35. Harutyunyan, E. H., Safonova, T. N., Kuranova, I. P., Popov, A. N., Teplyakov, A. V., Obmolova, G. V., Rusakov, A. A., Vainshtein, B. K., Dodson, G. G., Wilson, J. C., and Perutz, M. F. (1995) J. Mol. Biol. 251, 104-115.
36. Kabsch, W. (1976) Acta Crytstallogr., Sect. A 32, 922-923.
37. Yuen, P. S., and Nyburg, S. C. (1979) J. Appl. Crystallogr. 12, 258.
38. Gerstein, M., and Chothia, C. (1991) J. Mol. Biol. 220, 133-149.
39. Cox, J. M. (1967) J. Mol. Biol. 28, 151-156.
40. Lee, B., and Richards F. M. (1971) J. Mol. Biol. 55, 379-400.
41. Matthews, B. W. (1968) J. Mol. Biol. 33, 491-497.
42. Brünger, A. T. (1993) Acta Crystallogr. D49, 24-36.
43. Kleywegt, G. J., and Brünger, A. T. (1996) Structure 4, 897-904.
44. Kleywegt, G. J., and Jones T. A. (1995) Structure 3, 535-540.
45. Derewenda, Z. S., Lee, L., and Derewenda, U. (1995) J. Mol. Biol. 252, 248-262.
46. Kitagawa, T. (1992) Prog. Biophys. Mol. Biol. 58, 1-18.