8rc0

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Current revision (19:56, 29 May 2024) (edit) (undo)
 
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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=8rc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rc0 OCA], [https://pdbe.org/8rc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rc0 RCSB], [https://www.ebi.ac.uk/pdbsum/8rc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rc0 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=8rc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rc0 OCA], [https://pdbe.org/8rc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rc0 RCSB], [https://www.ebi.ac.uk/pdbsum/8rc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rc0 ProSAT]</span></td></tr>
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== Disease ==
 
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[https://www.uniprot.org/uniprot/PRP6_HUMAN PRP6_HUMAN] Retinitis pigmentosa. The disease may be caused by mutations affecting the gene represented in this entry. Cells from RP60 patients show intron retention for pre-mRNA bearing specific splicing signals.
 
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/PRP6_HUMAN PRP6_HUMAN] Involved in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation.<ref>PMID:12039962</ref>
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[https://www.uniprot.org/uniprot/CD2B2_HUMAN CD2B2_HUMAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 20S U5 small nuclear ribonucleoprotein particle (snRNP) is a 17-subunit RNA-protein complex and a precursor of the U4/U6.U5 tri-snRNP, the major building block of the precatalytic spliceosome. CD2BP2 is a hallmark protein of the 20S U5 snRNP, absent from the mature tri-snRNP. Here we report a high-resolution cryogenic electron microscopy structure of the 20S U5 snRNP, shedding light on the mutually exclusive interfaces utilized during tri-snRNP assembly and the role of the CD2BP2 in facilitating this process.
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Structure of the human 20S U5 snRNP.,Schneider S, Brandina I, Peter D, Lagad S, Fraudeau A, Portell-Montserrat J, Tholen J, Zhao J, Galej WP Nat Struct Mol Biol. 2024 May;31(5):752-756. doi: 10.1038/s41594-024-01250-5. , Epub 2024 Mar 11. PMID:38467877<ref>PMID:38467877</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8rc0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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<references/>

Current revision

Structure of the human 20S U5 snRNP

PDB ID 8rc0

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