4mhg: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:
{{STRUCTURE_4mhg|  PDB=4mhg  |  SCENE=  }}
==Crystal structure of ETV6 bound to a specific DNA sequence==
===Crystal structure of ETV6 bound to a specific DNA sequence===
<StructureSection load='4mhg' size='340' side='right' caption='[[4mhg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
{{ABSTRACT_PUBMED_24333486}}
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4mhg]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MHG FirstGlance]. <br>
==Function==
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lf8|2lf8]], [[2lf7|2lf7]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Etv6, Tel, Tel1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mhg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mhg RCSB], [http://www.ebi.ac.uk/pdbsum/4mhg PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/ETV6_MOUSE ETV6_MOUSE]] Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'.  
[[http://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 ==
DNA binding by the ETS transcriptional repressor ETV6 (or TEL) is auto-inhibited~50-fold due to an alpha-helix that sterically blocks its ETS domain binding interface. Using NMR spectroscopy, we demonstrate that this marginally-stable helix is unfolded, and not displaced to a non-inhibitory position, when ETV6 is bound to DNA containing a consensus 5'GGAA3' recognition site. Although significantly lower in affinity, binding to non-specific DNA is auto-inhibited~5-fold and also accompanied by helix unfolding. Based on NMR chemical shift perturbations, both specific and non-specific DNA are bound via the same canonical ETS domain interface. However, spectral perturbations are smaller for the non-specific complex, suggesting weaker and less well-defined interactions than in the specific complex. In parallel, the crystal structure of ETV6 bound to a specific DNA duplex was determined. The structure of this complex reveals that a non-conserved histidine residue in the ETS domain recognition helix helps establish the specificity of ETV6 for DNA-binding sites containing 5'GGAA3' versus 5'GGAT3'. These studies provide a unified steric mechanism for attenuating ETV6 binding to both specific and non-specific DNA and expand the repertoire of characterized auto-inhibitory strategies utilized to regulate ETS factors.


==About this Structure==
Steric mechanism of auto-inhibitory regulation of specific and non-specific DNA binding by the ETS transcriptional repressor ETV6.,De S, Chan AC, Coyne HJ 3rd, Bhachech N, Hermsdorf U, Okon M, Murphy ME, Graves BJ, McIntosh LP J Mol Biol. 2013 Dec 11. pii: S0022-2836(13)00747-X. doi:, 10.1016/j.jmb.2013.11.031. PMID:24333486<ref>PMID:24333486</ref>
[[4mhg]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MHG OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:024333486</ref><references group="xtra"/><references/>
</div>
[[Category: Chan, A C.]]
== References ==
[[Category: De, S.]]
<references/>
[[Category: Graves, B J.]]
__TOC__
[[Category: III, H J.Coyne.]]
</StructureSection>
[[Category: McIntosh, L P.]]
[[Category: Lk3 transgenic mice]]
[[Category: Murphy, M E.]]
[[Category: Chan, A C]]
[[Category: Okon, M.]]
[[Category: De, S]]
[[Category: Graves, B J]]
[[Category: III, H J.Coyne]]
[[Category: McIntosh, L P]]
[[Category: Murphy, M E]]
[[Category: Okon, M]]
[[Category: Ets domain]]
[[Category: Ets domain]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
[[Category: Transcription-dna complex]]
[[Category: Transcription-dna complex]]

Revision as of 23:23, 24 December 2014

Crystal structure of ETV6 bound to a specific DNA sequenceCrystal structure of ETV6 bound to a specific DNA sequence

Structural highlights

4mhg is a 3 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:Etv6, Tel, Tel1 (LK3 transgenic mice)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[ETV6_MOUSE] Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'.

Publication Abstract from PubMed

DNA binding by the ETS transcriptional repressor ETV6 (or TEL) is auto-inhibited~50-fold due to an alpha-helix that sterically blocks its ETS domain binding interface. Using NMR spectroscopy, we demonstrate that this marginally-stable helix is unfolded, and not displaced to a non-inhibitory position, when ETV6 is bound to DNA containing a consensus 5'GGAA3' recognition site. Although significantly lower in affinity, binding to non-specific DNA is auto-inhibited~5-fold and also accompanied by helix unfolding. Based on NMR chemical shift perturbations, both specific and non-specific DNA are bound via the same canonical ETS domain interface. However, spectral perturbations are smaller for the non-specific complex, suggesting weaker and less well-defined interactions than in the specific complex. In parallel, the crystal structure of ETV6 bound to a specific DNA duplex was determined. The structure of this complex reveals that a non-conserved histidine residue in the ETS domain recognition helix helps establish the specificity of ETV6 for DNA-binding sites containing 5'GGAA3' versus 5'GGAT3'. These studies provide a unified steric mechanism for attenuating ETV6 binding to both specific and non-specific DNA and expand the repertoire of characterized auto-inhibitory strategies utilized to regulate ETS factors.

Steric mechanism of auto-inhibitory regulation of specific and non-specific DNA binding by the ETS transcriptional repressor ETV6.,De S, Chan AC, Coyne HJ 3rd, Bhachech N, Hermsdorf U, Okon M, Murphy ME, Graves BJ, McIntosh LP J Mol Biol. 2013 Dec 11. pii: S0022-2836(13)00747-X. doi:, 10.1016/j.jmb.2013.11.031. PMID:24333486[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ De S, Chan AC, Coyne HJ 3rd, Bhachech N, Hermsdorf U, Okon M, Murphy ME, Graves BJ, McIntosh LP. Steric mechanism of auto-inhibitory regulation of specific and non-specific DNA binding by the ETS transcriptional repressor ETV6. J Mol Biol. 2013 Dec 11. pii: S0022-2836(13)00747-X. doi:, 10.1016/j.jmb.2013.11.031. PMID:24333486 doi:http://dx.doi.org/10.1016/j.jmb.2013.11.031

4mhg, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4mhg&oldid=2227124"