6l34

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Current revision (10:50, 22 November 2023) (edit) (undo)
 
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<StructureSection load='6l34' size='340' side='right'caption='[[6l34]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6l34' size='340' side='right'caption='[[6l34]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6l34]] 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=6L34 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L34 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6l34]] 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=6L34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L34 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSRP1, FACT80 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 1.996&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6l34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l34 OCA], [http://pdbe.org/6l34 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l34 RCSB], [http://www.ebi.ac.uk/pdbsum/6l34 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l34 ProSAT]</span></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=6l34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l34 OCA], [https://pdbe.org/6l34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l34 RCSB], [https://www.ebi.ac.uk/pdbsum/6l34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l34 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dou, Y S]]
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[[Category: Dou YS]]
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[[Category: Hu, T T]]
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[[Category: Hu TT]]
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[[Category: Li, H Y]]
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[[Category: Li HY]]
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[[Category: Su, D]]
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[[Category: Su D]]
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[[Category: Chaperone]]
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[[Category: Histone chaperone]]
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Current revision

Crystal structure of the HMG domain of human FACT complex subunit SSRP1

PDB ID 6l34

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