5e5b: Difference between revisions

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<StructureSection load='5e5b' size='340' side='right'caption='[[5e5b]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='5e5b' size='340' side='right'caption='[[5e5b]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5e5b]] is a 1 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=5E5B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E5B FirstGlance]. <br>
<table><tr><td colspan='2'>[[5e5b]] is a 1 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=5E5B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E5B FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SUPT16H, FACT140, FACTP140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5b OCA], [http://pdbe.org/5e5b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e5b RCSB], [http://www.ebi.ac.uk/pdbsum/5e5b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5b ProSAT]</span></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=5e5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5b OCA], [https://pdbe.org/5e5b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e5b RCSB], [https://www.ebi.ac.uk/pdbsum/5e5b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Huang, D T]]
[[Category: Huang DT]]
[[Category: Marciano, G]]
[[Category: Marciano G]]
[[Category: Aminopeptidase]]
[[Category: Chromatin]]
[[Category: Chromosomal protein]]
[[Category: Dna damage]]
[[Category: Dna repair]]
[[Category: Dna replication]]
[[Category: Fact]]
[[Category: Histone binding module]]
[[Category: Nucleus]]
[[Category: Pita-bread]]
[[Category: Replication]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
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