1kq8
From Proteopedia
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| - | [[Image:1kq8.jpg|left|200px]] | ||
| - | + | ==Solution Structure of Winged Helix Protein HFH-1== | |
| - | + | <StructureSection load='1kq8' size='340' side='right'caption='[[1kq8]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1kq8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQ8 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
| - | | | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq8 OCA], [https://pdbe.org/1kq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kq8 RCSB], [https://www.ebi.ac.uk/pdbsum/1kq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kq8 ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/FOXQ1_RAT FOXQ1_RAT] Plays a role in hair follicle differentiation (By similarity). | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kq/1kq8_consurf.spt"</scriptWhenChecked> | |
| - | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kq8 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The hepatocyte nuclear factor 3 (HNF-3)/fork head (fkh) family contains a large number of transcription factors that recognize divergent DNA sequences via a winged helix binding motif. HNF-3/fkh proteins show a broad profile of DNA sequence-specificity in which one DNA sequence can be recognized by more than one HNF-3/fkh protein and each individual HNF-3/fkh protein has several DNA binding sequences. In this study, heteronuclear NMR methods were used to study the structures of the DNA binding domain of a conserved winged helix protein HFH-1 and its DNA complexes. The structural comparison of winged helix proteins HFH-1 and Genesis and their DNA complexes indicates that even two highly conserved HNF-3 family members can adopt different local structures when they contact an identical DNA binding sequence, while one of these two HNF-3 proteins seems to adopt only slightly different structures on different DNA binding sites. | The hepatocyte nuclear factor 3 (HNF-3)/fork head (fkh) family contains a large number of transcription factors that recognize divergent DNA sequences via a winged helix binding motif. HNF-3/fkh proteins show a broad profile of DNA sequence-specificity in which one DNA sequence can be recognized by more than one HNF-3/fkh protein and each individual HNF-3/fkh protein has several DNA binding sequences. In this study, heteronuclear NMR methods were used to study the structures of the DNA binding domain of a conserved winged helix protein HFH-1 and its DNA complexes. The structural comparison of winged helix proteins HFH-1 and Genesis and their DNA complexes indicates that even two highly conserved HNF-3 family members can adopt different local structures when they contact an identical DNA binding sequence, while one of these two HNF-3 proteins seems to adopt only slightly different structures on different DNA binding sites. | ||
| - | + | Structure comparison of two conserved HNF-3/fkh proteins HFH-1 and genesis indicates the existence of folding differences in their complexes with a DNA binding sequence.,Sheng W, Rance M, Liao X Biochemistry. 2002 Mar 12;41(10):3286-93. PMID:11876636<ref>PMID:11876636</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1kq8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | + | [[Category: Liao X]] | |
| - | [[Category: Liao | + | [[Category: Rance M]] |
| - | [[Category: Rance | + | [[Category: Sheng W]] |
| - | [[Category: Sheng | + | |
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Current revision
Solution Structure of Winged Helix Protein HFH-1
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