1hkt
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hks|1HKS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hkt OCA], [http://www.ebi.ac.uk/pdbsum/1hkt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hkt RCSB]</span> | ||
}} | }} | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:06:53 2008'' |
Revision as of 18:06, 30 March 2008
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| Related: | 1HKS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR
Overview
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.
About this Structure
1HKT is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
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
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