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New page: left|200px<br /><applet load="2hfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hfh" /> '''THE NMR STRUCTURES OF A WINGED HELIX PROTEIN...
 
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[[Image:2hfh.jpg|left|200px]]<br /><applet load="2hfh" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2hfh.jpg|left|200px]]<br /><applet load="2hfh" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2hfh" />
caption="2hfh" />
'''THE NMR STRUCTURES OF A WINGED HELIX PROTEIN: GENESIS, 20 STRUCTURES'''<br />
'''THE NMR STRUCTURES OF A WINGED HELIX PROTEIN: GENESIS, 20 STRUCTURES'''<br />


==Overview==
==Overview==
The hepatocyte nuclear factor 3 (HNF-3)/fork head (fkh) family contains a, large number of transcription factors and folds into a winged helix motif., Despite having almost invariable amino acid sequences in their principal, DNA-binding helices, HNF-3/fkh proteins show a wide diversity of, sequence-specific binding. Previous studies of chimeric HNF-3/fkh proteins, demonstrated that the binding specificity is primarily influenced by a, region directly adjacent to the binding helix. We report our findings of, an NMR structural study performed on an HNF-3/fkh family member (Genesis, formerly HFH-2) and compare it to that of another family member, (HNF-3gamma) complexed to DNA and determined by X-ray crystallography. It, is found that in comparison to HNF-3gamma, Genesis contains an extra small, helix directly prior to the N terminus of the primary DNA contact helix., Due to the insertion of this helix, a shorter and slightly re-positioned, primary DNA contact helix is observed, which we believe leads to the, DNA-binding specificity differences among family members.
The hepatocyte nuclear factor 3 (HNF-3)/fork head (fkh) family contains a large number of transcription factors and folds into a winged helix motif. Despite having almost invariable amino acid sequences in their principal DNA-binding helices, HNF-3/fkh proteins show a wide diversity of sequence-specific binding. Previous studies of chimeric HNF-3/fkh proteins demonstrated that the binding specificity is primarily influenced by a region directly adjacent to the binding helix. We report our findings of an NMR structural study performed on an HNF-3/fkh family member (Genesis, formerly HFH-2) and compare it to that of another family member (HNF-3gamma) complexed to DNA and determined by X-ray crystallography. It is found that in comparison to HNF-3gamma, Genesis contains an extra small helix directly prior to the N terminus of the primary DNA contact helix. Due to the insertion of this helix, a shorter and slightly re-positioned primary DNA contact helix is observed, which we believe leads to the DNA-binding specificity differences among family members.


==About this Structure==
==About this Structure==
2HFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HFH OCA].  
2HFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HFH OCA].  


==Reference==
==Reference==
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[[Category: winged helix protein]]
[[Category: winged helix protein]]


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