5d8l

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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==
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<StructureSection load='5d8l' size='340' side='right' caption='[[5d8l]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
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<StructureSection load='5d8l' size='340' side='right'caption='[[5d8l]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d8k|5d8k]]</td></tr>
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</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>
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<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>
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<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>
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<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>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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==See Also==
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*[[Heat shock factor|Heat shock factor]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5d8l" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Jaeger, A M]]
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[[Category: Large Structures]]
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[[Category: Pemble, C W]]
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[[Category: Synthetic construct]]
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[[Category: Thiele, D J]]
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[[Category: Jaeger AM]]
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[[Category: Dna]]
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[[Category: Pemble CW]]
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[[Category: Hsf]]
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[[Category: Thiele DJ]]
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[[Category: Transcription factor]]
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[[Category: Transcription-dna complex]]
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Current revision

Human HSF2 DNA Binding Domain in complex with 3-site HSE DNA at 2.1 Angstroms Resolution

PDB ID 5d8l

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