8yjm

From Proteopedia

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m (Protected "8yjm" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 8yjm is ON HOLD
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==Structure of human SPT16 MD-CTD and MCM2 HBD chaperoning a histone H3-H4 tetramer and a single chain H2B-H2A chimera==
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<StructureSection load='8yjm' size='340' side='right'caption='[[8yjm]], [[Resolution|resolution]] 4.15&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8yjm]] is a 7 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=8YJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YJM FirstGlance]. <br>
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Description:
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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]] 4.15&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=8yjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yjm OCA], [https://pdbe.org/8yjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yjm RCSB], [https://www.ebi.ac.uk/pdbsum/8yjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yjm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SP16H_HUMAN SP16H_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).<ref>PMID:10912001</ref> <ref>PMID:11239457</ref> <ref>PMID:12934006</ref> <ref>PMID:16713563</ref> <ref>PMID:9489704</ref> <ref>PMID:9836642</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Gan SL]]
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[[Category: Xu RM]]
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[[Category: Yang WS]]

Revision as of 08:22, 20 March 2024

Structure of human SPT16 MD-CTD and MCM2 HBD chaperoning a histone H3-H4 tetramer and a single chain H2B-H2A chimera

PDB ID 8yjm

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