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New page: left|200px<br /><applet load="1hkt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hkt" /> '''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN...
 
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[[Image:1hkt.jpg|left|200px]]<br /><applet load="1hkt" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hkt.jpg|left|200px]]<br /><applet load="1hkt" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hkt" />
caption="1hkt" />
'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR'''<br />
'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF DROSOPHILA HEAT SHOCK TRANSCRIPTION FACTOR'''<br />


==Overview==
==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.
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==
==About this Structure==
1HKT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HKT OCA].  
1HKT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HKT OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bax, A.]]
[[Category: Bax, A.]]
[[Category: Kim, S.J.]]
[[Category: Kim, S J.]]
[[Category: Marquardt, J.L.]]
[[Category: Marquardt, J L.]]
[[Category: Orosz, A.]]
[[Category: Orosz, A.]]
[[Category: Vuister, G.W.]]
[[Category: Vuister, G W.]]
[[Category: Wu, C.]]
[[Category: Wu, C.]]
[[Category: transcription regulation]]
[[Category: transcription regulation]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:37:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:20 2008''