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Crystal Structure of the DNA Binding Domain of the Heat Shock Transcription Factor
Abstract
The structure of the DNA binding domain, determined at 1.8 angstrom resolution, contains a three-helix bundle that is capped by a four-stranded antiparallel β sheet. This structure is a variant of the helix-turn-helix motif, typified by catabolite activator protein. In the heat shock transcription factor, the first helix of the motif (α2) has an α-helical bulge and a proline-induced kink. The angle between the two helices of the motif (α2 and α3) is about 20° smaller than the average for canonical helix-turn-helix proteins. Nevertheless, the relative positions of the first and third helices of the bundle (α1 and α3) are conserved. It is proposed here that the first helix of the three-helix bundle be considered a component of the helix-turn-helix motif.
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Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Sorger, P. K., & Pelham, H. R. B. (1988) · Cell · doi:10.1016/s0092-8674(88)91219-6 · Cited by 832
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Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.24.3788 · Cited by 1,906
Heat shock factors: integrators of cell stress, development and lifespan
Åkerfelt, M., Morimoto, R. I., & Sistonen, L. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2938 · Cited by 1,455
Nover, L., Bharti, K., Döring, P., Mishra, S. K., Ganguli, A., & Scharf, K.-D. (2001) · Cell Stress & Chaperones · doi:10.1379/1466-1268(2001)006<0177:aathst>2.0.co;2 · Cited by 769
Baniwal, S. K., Bharti, K., Chan, K. Y., Fauth, M., Ganguli, A., Kotak, S., Mishra, S. K., Nover, L., Port, M., Scharf, K.-D., et al. (2004) · Journal of Biosciences · doi:10.1007/bf02712120 · Cited by 600
Binding of the winged-helix transcription factor HNF3 to a linker histone site on the nucleosome
Cirillo, L. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.1.244 · Cited by 381
Metadata
- Authors
- Harrison, C. J., Bohm, A. A., & Nelson, H. C. M.
- Venue
- Science
- Published
- 1994-01-14
- Volume
- 263
- Issue
- 5144
- Pages
- 224-227
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2089176336
- Cited by
- 269
- References
- 2
- FWCI
- 8.09
- Type
- journal article
- Language
- en
- Open access
- closed
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