2lf7: Difference between revisions
New page: '''Unreleased structure''' The entry 2lf7 is ON HOLD Authors: Coyne, H., III, Green, S.M., Graves, B.J., McIntosh, L.P. Description: Q436 |
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The | ==Intramolecular regulation of the ETS Domain within ETV6 sequence R335 to Q436== | ||
<StructureSection load='2lf7' size='340' side='right'caption='[[2lf7]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lf7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LF7 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=2lf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lf7 OCA], [https://pdbe.org/2lf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lf7 RCSB], [https://www.ebi.ac.uk/pdbsum/2lf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lf7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ETV6_MOUSE ETV6_MOUSE] Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ETV6 (or TEL), a transcriptional repressor belonging to the ETS family, is frequently involved in chromosomal translocations linked with human cancers. It displays a DNA-binding mode distinct from other ETS proteins due to the presence of a self-associating PNT domain. In this study, we used NMR spectroscopy to dissect the structural and dynamic bases for the autoinhibition of ETV6 DNA binding by sequences C-terminal to its ETS domain. The C-terminal inhibitory domain (CID) contains two helices, H4 and H5, which sterically block the DNA-binding interface of the ETS domain. Importantly, these appended helices are only marginally stable as revealed by amide hydrogen exchange and (15)N relaxation measurements. The CID is thus poised to undergo a facile conformational change as required for DNA binding. The CID also dampens millisecond timescale motions of the ETS domain hypothesized to be critical for the recognition of specific ETS target sequences. This work illustrates the use of appended sequences on conserved structural domains to generate biological diversity and complements previous studies of the allosteric mechanism of ETS1 autoinhibition to reveal both common and divergent features underlying the regulation of DNA binding by ETS transcription factors. | |||
Autoinhibition of ETV6 (TEL) DNA Binding: Appended Helices Sterically Block the ETS Domain.,Coyne HJ 3rd, De S, Okon M, Green SM, Bhachech N, Graves BJ, McIntosh LP J Mol Biol. 2012 Aug 3;421(1):67-84. Epub 2012 May 12. PMID:22584210<ref>PMID:22584210</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lf7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Coyne III H]] | |||
[[Category: Graves BJ]] | |||
[[Category: Green SM]] | |||
[[Category: Mcintosh LP]] | |||