5d5u

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==Crystal structure of human Hsf1 with HSE DNA==
==Crystal structure of human Hsf1 with HSE DNA==
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<StructureSection load='5d5u' size='340' side='right' caption='[[5d5u]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
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<StructureSection load='5d5u' size='340' side='right'caption='[[5d5u]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5d5u]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D5U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5d5u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D5U FirstGlance]. <br>
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</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=5d5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5u OCA], [http://pdbe.org/5d5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d5u RCSB], [http://www.ebi.ac.uk/pdbsum/5d5u PDBsum]</span></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]] 2.91&#8491;</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=5d5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5u OCA], [https://pdbe.org/5d5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d5u RCSB], [https://www.ebi.ac.uk/pdbsum/5d5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d5u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HSF1_HUMAN HSF1_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.<ref>PMID:11447121</ref> <ref>PMID:8946918</ref> <ref>PMID:9121459</ref> <ref>PMID:9535852</ref> <ref>PMID:11583998</ref> <ref>PMID:12659875</ref> <ref>PMID:12665592</ref> <ref>PMID:16278218</ref>
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[https://www.uniprot.org/uniprot/HSF1_HUMAN HSF1_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.<ref>PMID:11447121</ref> <ref>PMID:8946918</ref> <ref>PMID:9121459</ref> <ref>PMID:9535852</ref> <ref>PMID:11583998</ref> <ref>PMID:12659875</ref> <ref>PMID:12665592</ref> <ref>PMID:16278218</ref>
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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 1 (HSF1) has a central role in mediating the protective response to protein conformational stresses in eukaryotes. HSF1 consists of an N-terminal DNA-binding domain (DBD), a coiled-coil oligomerization domain, a regulatory domain and a transactivation domain. Upon stress, HSF1 trimerizes via its coiled-coil domain and binds to the promoters of heat shock protein-encoding genes. Here, we present cocrystal structures of the human HSF1 DBD in complex with cognate DNA. A comparative analysis of the HSF1 paralog Skn7 from Chaetomium thermophilum showed that single amino acid changes in the DBD can switch DNA binding specificity, thus revealing the structural basis for the interaction of HSF1 with cognate DNA. We used a crystal structure of the coiled-coil domain of C. thermophilum Skn7 to develop a model of the active human HSF1 trimer in which HSF1 embraces the heat-shock-element DNA.
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Structure of human heat-shock transcription factor 1 in complex with DNA.,Neudegger T, Verghese J, Hayer-Hartl M, Hartl FU, Bracher A Nat Struct Mol Biol. 2016 Jan 4. doi: 10.1038/nsmb.3149. PMID:26727489<ref>PMID:26727489</ref>
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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 5d5u" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Heat shock factor|Heat shock factor]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bracher, A]]
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[[Category: Homo sapiens]]
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[[Category: Double helix]]
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[[Category: Large Structures]]
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[[Category: Helix-turn-helix]]
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[[Category: Bracher A]]
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[[Category: Protein-dna complex]]
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[[Category: Hartl FU]]
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[[Category: Transcription-dna complex]]
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[[Category: Hayer-Hartl M]]
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[[Category: Neudegger T]]
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[[Category: Verghese J]]

Current revision

Crystal structure of human Hsf1 with HSE DNA

PDB ID 5d5u

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