4ifs

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{{STRUCTURE_4ifs| PDB=4ifs | SCENE= }}
 
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===Crystal structure of the hSSRP1 Middle domain===
 
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==Function==
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==Crystal structure of the hSSRP1 Middle domain==
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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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<StructureSection load='4ifs' size='340' side='right'caption='[[4ifs]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[4ifs]] 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=4IFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IFS FirstGlance]. <br>
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[[4ifs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IFS OCA].
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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]] 1.93&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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==Reference==
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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=4ifs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ifs OCA], [https://pdbe.org/4ifs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ifs RCSB], [https://www.ebi.ac.uk/pdbsum/4ifs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ifs ProSAT]</span></td></tr>
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<references group="xtra"/><references/>
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</table>
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[[Category: Li, X.]]
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== Function ==
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[[Category: Liu, Y W.]]
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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>
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[[Category: Niu, L W.]]
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== References ==
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[[Category: Shao, C.]]
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<references/>
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[[Category: Teng, M K.]]
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__TOC__
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[[Category: Zeng, F X.]]
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</StructureSection>
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[[Category: Zhang, W J.]]
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[[Category: Homo sapiens]]
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[[Category: Chaperone]]
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[[Category: Large Structures]]
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[[Category: Double ph domain]]
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[[Category: Li X]]
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[[Category: Histone]]
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[[Category: Liu YW]]
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[[Category: Nucleus]]
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[[Category: Niu LW]]
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[[Category: Replication]]
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[[Category: Shao C]]
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[[Category: Transcription]]
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[[Category: Teng MK]]
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[[Category: Zeng FX]]
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[[Category: Zhang WJ]]

Current revision

Crystal structure of the hSSRP1 Middle domain

PDB ID 4ifs

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