View source for 8zys


==Crystal structure of HSF5 DNA-binding domain in complex with 3-site HSE DNA (25 bp)==
<StructureSection load='8zys' size='340' side='right'caption='[[8zys]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8zys]] is a 10 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=8ZYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZYS FirstGlance]. <br>
</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&#8491;</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=8zys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zys OCA], [https://pdbe.org/8zys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zys RCSB], [https://www.ebi.ac.uk/pdbsum/8zys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zys ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSF5_HUMAN HSF5_HUMAN] DNA-binding transcription factor that is essential for male fertility, spermatogenesis and meiotic prophase progression in spermatocytes under non-stress conditions. Positvely and negatively regulates gene expression to ensure progression of meiotic prophase beyond pachytene stage in spermatocytes. Plays a role in male germline meiotic sex chromosome remodeling and silencing through regulation of SMARCA4.[UniProtKB:Q5ND04]
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== Publication Abstract from PubMed ==
Heat shock factor 1 (HSF1) and 2 (HSF2) play distinct but overlapping regulatory roles in maintaining cellular proteostasis or mediating cell differentiation and development. Upon activation, both HSFs trimerize and bind to heat shock elements (HSEs) present in the promoter region of target genes. Despite structural insights gained from recent studies, structures reflecting the physiological architecture of this transcriptional machinery remains to be determined. Here, we present co-crystal structures of human HSF1 and HSF2 trimers bound to DNA, which reveal a triangular arrangement of the three DNA-binding domains (DBDs) with protein-protein interactions largely mediated by the wing domain. Two structural properties, different flexibility of the wing domain and local DNA conformational changes induced by HSF binding, seem likely to contribute to the subtle differential specificity between HSF1 and HSF2. Besides, two more structures showing DBDs bound to "two-site" head-to-head HSEs were determined as additions to the published tail-to-tail dimer-binding structures.

Structures of heat shock factor trimers bound to DNA.,Feng N, Feng H, Wang S, Punekar AS, Ladenstein R, Wang DC, Zhang Q, Ding J, Liu W iScience. 2021 Aug 5;24(9):102951. doi: 10.1016/j.isci.2021.102951. eCollection , 2021 Sep 24. PMID:34458700<ref>PMID:34458700</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8zys" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Liu W]]
[[Category: Shi X]]
[[Category: Zhang Q]]