Exploring the role of glutamine 50 in the homeodomain-DNA interface: Crystal structure of engrailed (Gln50 → Ala) complex at 2.0 Å

Biochemistry

Volumn 39, Issue 28, 2000, Pages 8187-8192

  Grant, Robert A ^a,b   Rould, Mark A ^a,b,c   Klemm, Juli D ^b,d   Pabo, Carl O ^a,b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c UNIVERSITY OF VERMONT COLLEGE OF MEDICINE   (United States)

^d Drug Metabolism Pharmacokinetics Clinical Pharmacology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; GLUTAMINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN DNA INTERACTION;

CRYSTALLOGRAPHY; DNA; GLUTAMINE; HOMEODOMAIN PROTEINS; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; PEPTIDES; PROTEIN CONFORMATION; TATA BOX;

EID: 0034682619     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi000071a     Document Type: Article

References (27)

1. Hanes, S. D., and Brent, R. (1989) Cell 57, 1275-1283.
2. Hanes, S. D., and Brent, R. (1991) Science 251, 426-430.
3. Treisman, J., Gonczy, P., Vashishtha, M., Harris, E., and Desplan, C. (1989) Cell 59, 553-562.
4. Percival-Smith, A., Muller, M., Affolter, M., and Gehring, W. J. (1990) EMBO J. 9, 3967-3974.
5. Billeter, M., Qian, Y. Q., Otting, G., Muller, M., Gehring, W., and Wuthrich, K. (1993) J. Mol. Biol. 234, 1084-1093.
6. Hirsch, J. A., and Aggarwal, A. K. (1995) EMBO J. 14, 6280-6291.
7. Fraenkel, E., Rould, M. A., Chambers, K. A., and Pabo, C. O. (1998) J. Mol. Biol. 284, 351-361.
8. Fraenkel, E., and Pabo, C. O. (1998) Nat. Struct. Biol. 5, 692-697.
9. Wolberger, C. (1996) Curr. Opin. Struct. Biol. 6, 62-68.
10. Qian, Y. Q., Billeter, M., Otting, G., Muller, M., Gehring, W. J., and Wuthrich, K. (1989) Cell 59, 573-580.
11. Qian, Y. Q., Furukubo-Tokunaga, K., Resendez-Perez, D., Muller, M., Gehring, W. J., and Wuthrich, K. (1994) J. Mol. Biol. 238, 333-345.
12. Gehring, W. J., Affolter, M., and Burglin, T. (1994) Annu. Rev. Biochem. 63, 487-526.
13. Pabo, C. O., and Sauer, R. T. (1984) Annu. Rev. Biochem. 53, 293-321.
14. Ades, S. E., and Sauer, R. T. (1994) Biochemistry 33, 9187-9194.
15. Schwabe, J. W. (1997) Curr. Opin. Struct. Biol. 7, 126-134.
16. Labeots, L. A., and Weiss, M. A. (1997) J. Mol. Biol. 269, 113-128.
17. Wilson, D. S., Guenther, B., Desplan, C., and Kuriyan, J. (1995) Cell 82, 709-719.
18. Wilson, D. S., Sheng, G., Jun, S., and Desplan, C. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 6886-6891.
19. Kissinger, C. R., Liu, B. S., Martin-Blanco, E., Kornberg, T. B., and Pabo, C. O. (1990) Cell 63, 579-590.
20. Otwinowski, Z., and Minor, W. (1996) in Methods in Enzymology (Carter, C., and Sweet, R. M., Eds.) pp 307-326, Academic Press, New York.
21. Tucker-Kellogg, L., Rould, M. A., Chambers, K. A., Ades, S. E., Sauer, R. T., and Pabo, C. O. (1997) Structure 5, 1047-1054.
22. Brunger, A. T. (1992) X-PLOR Manual Version 3.1, Yale University Press, New Haven, CT.
23. Lavery, R., and Sklenar, H. (1988) J. Biomol. Struct. Dyn. 6, 63-91.
24. Stofer, E., and Lavery, R. (1994) Biopolymers 34, 337-346.
25. Passner, J. M., Ryoo, H. D., Shen, L., Mann, R. S., and Aggarwal, A. K. (1999) Nature 397, 714-719.
26. Piper, D. E., Batchelor, A. H., Chang, C. P., Cleary, M. L., and Wolberger, C. (1999) Cell 96, 587-597.
27. Gruschus, J. M., Tsao, D. H. H., Wang, L., Nirenberg, M., and Ferretti, I. A. (1997) Biochemistry 36, 5372-5380.