1hkt

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{{Structure
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|RELATEDENTRY=[[1hks|1HKS]]
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|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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'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR'''
'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR'''
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[[Category: Vuister, G W.]]
[[Category: Vuister, G W.]]
[[Category: Wu, C.]]
[[Category: Wu, C.]]
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[[Category: transcription regulation]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:57:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:06:53 2008''
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Revision as of 15:57, 2 May 2008

Template:STRUCTURE 1hkt

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 Page seeded by OCA on Fri May 2 18:57:21 2008

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