View source for 6upl


==Structure of FACT_subnucleosome complex 2==
<SX load='6upl' size='340' side='right' viewer='molstar' caption='[[6upl]], [[Resolution|resolution]] 7.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6upl]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UPL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.4&#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=6upl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6upl OCA], [https://pdbe.org/6upl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6upl RCSB], [https://www.ebi.ac.uk/pdbsum/6upl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6upl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SSRP1_HUMAN SSRP1_HUMAN] Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.<ref>PMID:9489704</ref> <ref>PMID:9566881</ref> <ref>PMID:9836642</ref> <ref>PMID:10912001</ref> <ref>PMID:11239457</ref> <ref>PMID:12374749</ref> <ref>PMID:12934006</ref> <ref>PMID:16713563</ref> 

==See Also==
*[[Histone 3D structures|Histone 3D structures]]
== References ==
<references/>
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</SX>
[[Category: Escherichia coli]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Carragher B]]
[[Category: Liu Y]]
[[Category: Luger K]]
[[Category: Potter C]]
[[Category: Tan YZ]]
[[Category: Wei H]]
[[Category: Zhou K]]