View source for 2m9h


==DNA-binding domain of T. brucei telomeric protein tbTRF==
<StructureSection load='2m9h' size='340' side='right'caption='[[2m9h]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M9H 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=2m9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m9h OCA], [https://pdbe.org/2m9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m9h RCSB], [https://www.ebi.ac.uk/pdbsum/2m9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m9h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q4VHG6_9TRYP Q4VHG6_9TRYP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Trypanosoma brucei causes human African trypanosomiasis and regularly switches its major surface antigen, VSG, in the bloodstream of its mammalian host to evade the host immune response. VSGs are expressed exclusively from subtelomeric loci, and we have previously shown that telomere proteins TbTIF2 and TbRAP1 play important roles in VSG switching and VSG silencing regulation, respectively. We now discover that the telomere duplex DNA-binding factor, TbTRF, also plays a critical role in VSG switching regulation, as a transient depletion of TbTRF leads to significantly more VSG switching events. We solved the NMR structure of the DNA-binding Myb domain of TbTRF, which folds into a canonical helix-loop-helix structure that is conserved to the Myb domains of mammalian TRF proteins. The TbTRF Myb domain tolerates well the bulky J base in T. brucei telomere DNA, and the DNA-binding affinity of TbTRF is not affected by the presence of J both in vitro and in vivo. In addition, we find that point mutations in TbTRF Myb that significantly reduced its in vivo telomere DNA-binding affinity also led to significantly increased VSG switching frequencies, indicating that the telomere DNA-binding activity is critical for TbTRF's role in VSG switching regulation.

Suppression of subtelomeric VSG switching by Trypanosoma brucei TRF requires its TTAGGG repeat-binding activity.,Jehi SE, Li X, Sandhu R, Ye F, Benmerzouga I, Zhang M, Zhao Y, Li B Nucleic Acids Res. 2014 Nov 10;42(20):12899-911. doi: 10.1093/nar/gku942. Epub, 2014 Oct 13. PMID:25313155<ref>PMID:25313155</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m9h" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trypanosoma brucei]]
[[Category: Li X]]
[[Category: Ye F]]
[[Category: Zhang M]]
[[Category: Zhao Y]]