2v1n: Difference between revisions

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[[Image:2v1n.png|left|200px]]
==SOLUTION STRUCTURE OF THE REGION 51-160 OF HUMAN KIN17 REVEALS A WINGED HELIX FOLD==
<StructureSection load='2v1n' size='340' side='right' caption='[[2v1n]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2v1n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V1N FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ckk|2ckk]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v1n RCSB], [http://www.ebi.ac.uk/pdbsum/2v1n PDBsum]</span></td></tr>
<table>
== 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/v1/2v1n_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human KIN17 is a 45-kDa eukaryotic DNA- and RNA-binding protein that plays an important role in nuclear metabolism and in particular in the general response to genotoxics. Its amino acids sequence contains a zinc finger motif (residues 28-50) within a 30-kDa N-terminal region conserved from yeast to human, and a 15-kDa C-terminal tandem of SH3-like subdomains (residues 268-393) only found in higher eukaryotes. Here we report the solution structure of the region 51-160 of human KIN17. We show that this fragment folds into a three-alpha-helix bundle packed against a three-stranded beta-sheet. It belongs to the winged helix (WH) family. Structural comparison with analogous WH domains reveals that KIN17 WH module presents an additional and highly conserved 3(10)-helix. Moreover, KIN17 WH helix H3 is not positively charged as in classical DNA-binding WH domains. Thus, human KIN17 region 51-160 might rather be involved in protein-protein interaction through its conserved surface centered on the 3(10)-helix.


{{STRUCTURE_2v1n|  PDB=2v1n  |  SCENE=  }}
Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain.,Carlier L, Couprie J, le Maire A, Guilhaudis L, Milazzo-Segalas I, Courcon M, Moutiez M, Gondry M, Davoust D, Gilquin B, Zinn-Justin S Protein Sci. 2007 Dec;16(12):2750-5. PMID:18029424<ref>PMID:18029424</ref>


===SOLUTION STRUCTURE OF THE REGION 51-160 OF HUMAN KIN17 REVEALS A WINGED HELIX FOLD===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_18029424}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2v1n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1N OCA].
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Carlier, L.]]
[[Category: Carlier, L.]]

Revision as of 02:21, 1 October 2014

SOLUTION STRUCTURE OF THE REGION 51-160 OF HUMAN KIN17 REVEALS A WINGED HELIX FOLD

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