Disordered tails of homeodomains facilitate DNA recognition by providing a trade-off between folding and specific binding

Journal of the American Chemical Society

Volumn 131, Issue 42, 2009, Pages 15084-15085

  Tóth Petróczy, Ágnes ^a,b   Simon, Istvan ^b   Fuxreiter, Monika ^b   Levy, Yaakov ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; BINDING PROCESS; BINDING STRENGTH; COARSE-GRAINED MOLECULAR DYNAMICS SIMULATIONS; DISORDERED STATE; DNA BINDING; DNA RECOGNITION; DNA-BINDING SPECIFICITY; HOMEODOMAIN; HOMEODOMAIN TRANSCRIPTION FACTOR; INTRAMOLECULAR INTERACTIONS; KINETICS AND THERMODYNAMICS; MOLECULAR BASIS; N-TERMINALS; NATIVE PROTEINS; PROTEIN-DNA INTERFACE; RADIUS OF GYRATION; SPECIFIC BINDING; SPECIFIC INTERACTION;

BINDING ENERGY; DNA; GENES; MOLECULAR DYNAMICS; NUCLEIC ACIDS; PROTEIN FOLDING; TRANSCRIPTION FACTORS;

DNA SEQUENCES;

ANTENNAPEDIA PROTEIN; DNA; HOMEODOMAIN PROTEIN; PROTEIN; PROTEIN NK2; UNCLASSIFIED DRUG; WATER;

ARTICLE; BINDING AFFINITY; ELECTRICITY; ENTHALPY; ENTROPY; HEAT; HYDROPHOBICITY; MOLECULAR MODEL; MOLECULAR RECOGNITION; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN TARGETING; TRANSITION TEMPERATURE;

ANIMALS; ANTENNAPEDIA HOMEODOMAIN PROTEIN; DNA; DROSOPHILA PROTEINS; HOMEODOMAIN PROTEINS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS; TRANSCRIPTION FACTORS;

EID: 70350321301     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9052784     Document Type: Article

References (17)

1. Spolar, R. S.; Record, M. T., Jr. Science 1994, 263, 777.
2. Billeter, M.; Qian, Y. Q.; Otting, G.; Muller, M.; Gehring, W.; Wuthrich, K. J. Mol. Biol. 1993, 234, 1084.
3. Damante, G.; Di Lauro, R. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 5388.
4. Gruschus, J. M.; Tsao, D. H.; Wang, L. H.; Nirenberg, M.; Ferretti, J. A. Biochemistry 1997, 36, 5372.
5. Zeng, W. L.; Andrew, D. J.; Mathies, L. D.; Horner, M. A.; Scott, M. P. Development 1993, 118, 339.
6. Joshi, R.; Passner, J. M.; Rohs, R.; Jain, R.; Sosinsky, A.; Crickmore, M. A.; Jacob, V.; Aggarwal, A. K.; Honig, B.; Mann, R. S. Cell 2007, 131, 530.
7. Levy, Y.; Onuchic, J. N.; Wolynes, P. G. J. Am. Chem. Soc. 2007, 129, 738.
8. Crane-Robinson, C.; Dragan, A. I.; Privalov, P. L. Trends Biochem. Sci. 2006, 31, 547.
9. Levy, Y.; Cho, S. S.; Onuchic, J. N.; Wolynes, P. G. J. Mol. Biol. 2005, 346, 1121.
10. Turjanski, A. G.; Gutkind, J. S.; Best, R. B.; Hummer, G. PLoS Comput Biol 2008, 4, e1000060.
11. Dragan, A. I.; Li, Z.; Makeyeva, E. N.; Milgotina, E. I.; Liu, Y.; Crane-Robinson, C.; Privalov, P. L. Biochemistry 2006, 45, 141.
12. Shoemaker, B. A.; Portman, J. J.; Wolynes, P. G. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 8868.
13. Marcovitz, A.; Levy, Y. Biophys. J. 2009, 96, 4212.
14. Fuxreiter, M.; Mezei, M.; Simon, I.; Osman, R. Biophys. J. 2005, 89, 903.
15. Jana, B.; Pal, S.; Maiti, P. K.; Lin, S. T.; Hynes, J. T.; Bagchi, B. J. Phys. Chem. B 2006, 110, 19611.
16. Givaty, O.; Levy, Y. J. Mol. Biol. 2009, 385, 1087.
17. Kim, Y. C.; Tang, C.; Clore, G. M.; Hummer, G. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 12855.