28xb: Difference between revisions
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==Cryo-EM structure of the human UAP56-RNA - LENG8-PCID2-SEM1 complex== | |||
<StructureSection load='28xb' size='340' side='right'caption='[[28xb]], [[Resolution|resolution]] 6.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[28xb]] is a 5 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=28XB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=28XB 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]] 6.2Å</td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=28xb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=28xb OCA], [https://pdbe.org/28xb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=28xb RCSB], [https://www.ebi.ac.uk/pdbsum/28xb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=28xb ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: Graf | == Disease == | ||
[[Category: Plaschka | [https://www.uniprot.org/uniprot/SEM1_HUMAN SEM1_HUMAN] Split hand-split foot malformation. | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SEM1_HUMAN SEM1_HUMAN] Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (PubMed:15117943). Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3 (PubMed:22307388). The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and thus transcription-associated genomic instability. R-loop accumulation increases in SEM1-depleted cells.<ref>PMID:1317798</ref> <ref>PMID:15117943</ref> <ref>PMID:22307388</ref> <ref>PMID:24896180</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Graf M]] | |||
[[Category: Hohmann U]] | |||
[[Category: Plaschka C]] | |||
Latest revision as of 04:29, 24 June 2026
Cryo-EM structure of the human UAP56-RNA - LENG8-PCID2-SEM1 complex
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