Structural highlights
Function
HSF_DROME DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The solution structure of the DNA-binding domain of the Drosophila heat shock transcription factor, as determined by multidimensional multinuclear NMR, resembles that of the helix-turn-helix class of DNA-binding proteins. The domain comprises a four-stranded antiparallel beta-sheet, packed against a three-helix bundle. The second helix is significantly distorted and is separated from the third helix by an extended turn which is subject to conformational averaging on an intermediate time scale. Helix 3 forms a classical amphipathic helix with polar and charged residues exposed to the solvent. Upon titration with DNA, resonance shifts in the backbone and Asn and Gln side-chain amides indicate that helix 3 acts as the recognition helix of the heat shock transcription factor.
Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor.,Vuister GW, Kim SJ, Orosz A, Marquardt J, Wu C, Bax A Nat Struct Biol. 1994 Sep;1(9):605-14. PMID:7634100[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vuister GW, Kim SJ, Orosz A, Marquardt J, Wu C, Bax A. Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. Nat Struct Biol. 1994 Sep;1(9):605-14. PMID:7634100
