5d8l: Difference between revisions

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==Human HSF2 DNA Binding Domain in complex with 3-site HSE DNA at 2.1 Angstroms Resolution==
==Human HSF2 DNA Binding Domain in complex with 3-site HSE DNA at 2.1 Angstroms Resolution==
<StructureSection load='5d8l' size='340' side='right' caption='[[5d8l]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
<StructureSection load='5d8l' size='340' side='right'caption='[[5d8l]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5d8l]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D8L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D8L FirstGlance]. <br>
<table><tr><td colspan='2'>[[5d8l]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D8L FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d8k|5d8k]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.069&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSF2, HSTF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5d8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d8l OCA], [https://pdbe.org/5d8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d8l RCSB], [https://www.ebi.ac.uk/pdbsum/5d8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d8l ProSAT]</span></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=5d8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d8l OCA], [http://pdbe.org/5d8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d8l RCSB], [http://www.ebi.ac.uk/pdbsum/5d8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d8l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HSF2_HUMAN HSF2_HUMAN]] DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
[https://www.uniprot.org/uniprot/HSF2_HUMAN HSF2_HUMAN] DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Heat-shock transcription factor (HSF) family members function in stress protection and in human diseases including proteopathies, neurodegeneration and cancer. The mechanisms that drive distinct post-translational modifications, cofactor recruitment and target-gene activation for specific HSF paralogs are unknown. We present crystal structures of the human HSF2 DNA-binding domain (DBD) bound to DNA, revealing an unprecedented view of HSFs that provides insights into their unique biology. The HSF2 DBD structures resolve a new C-terminal helix that directs wrapping of the coiled-coil domain around DNA, thereby exposing paralog-specific sequences of the DBD surface for differential post-translational modifications and cofactor interactions. We further demonstrate a direct interaction between HSF1 and HSF2 through their coiled-coil domains. Together, these features provide a new model for HSF structure as the basis for differential and combinatorial regulation, which influences the transcriptional response to cellular stress.


Structures of HSF2 reveal mechanisms for differential regulation of human heat-shock factors.,Jaeger AM, Pemble CW 4th, Sistonen L, Thiele DJ Nat Struct Mol Biol. 2016 Jan 4. doi: 10.1038/nsmb.3150. PMID:26727490<ref>PMID:26727490</ref>
==See Also==
 
*[[Heat shock factor|Heat shock factor]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5d8l" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Jaeger, A M]]
[[Category: Large Structures]]
[[Category: Pemble, C W]]
[[Category: Synthetic construct]]
[[Category: Thiele, D J]]
[[Category: Jaeger AM]]
[[Category: Dna]]
[[Category: Pemble CW]]
[[Category: Hsf]]
[[Category: Thiele DJ]]
[[Category: Transcription factor]]
[[Category: Transcription-dna complex]]
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