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| | ==Structure of a human Prp31-15.5K-U4 snRNA complex== | | ==Structure of a human Prp31-15.5K-U4 snRNA complex== |
| - | <StructureSection load='2ozb' size='340' side='right' caption='[[2ozb]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='2ozb' size='340' side='right'caption='[[2ozb]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ozb]] is a 6 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=2OZB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OZB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ozb]] is a 6 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=2OZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OZB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e7k|1e7k]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NHP2L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PRPF31, PRP31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2ozb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ozb OCA], [https://pdbe.org/2ozb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ozb RCSB], [https://www.ebi.ac.uk/pdbsum/2ozb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ozb ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ozb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ozb OCA], [http://pdbe.org/2ozb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ozb RCSB], [http://www.ebi.ac.uk/pdbsum/2ozb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ozb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/PRP31_HUMAN PRP31_HUMAN]] Defects in PRPF31 are the cause of retinitis pigmentosa type 11 (RP11) [MIM:[http://omim.org/entry/600138 600138]]. RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP11 inheritance is autosomal dominant.<ref>PMID:17412961</ref> <ref>PMID:12444105</ref> <ref>PMID:11545739</ref> <ref>PMID:8808602</ref> <ref>PMID:12923864</ref> | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRP31_HUMAN PRP31_HUMAN]] Involved in pre-mRNA splicing. Required for U4/U6.U5 tri-snRNP formation.<ref>PMID:11867543</ref> [[http://www.uniprot.org/uniprot/NH2L1_HUMAN NH2L1_HUMAN]] Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding.<ref>PMID:10545122</ref> <ref>PMID:17412961</ref> | + | [https://www.uniprot.org/uniprot/NH2L1_HUMAN NH2L1_HUMAN] Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding.<ref>PMID:10545122</ref> <ref>PMID:17412961</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[15.5kD/Snu13/L7Ae protein|15.5kD/Snu13/L7Ae protein]] | + | *[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] |
| | + | *[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Liu, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Luehrmann, R]] | + | [[Category: Liu S]] |
| - | [[Category: Wahl, M C]] | + | [[Category: Luehrmann R]] |
| - | [[Category: Hierarchical assembly]] | + | [[Category: Wahl MC]] |
| - | [[Category: Nop domain]]
| + | |
| - | [[Category: Pre-mrna splicing]]
| + | |
| - | [[Category: Rna binding protein-rna complex]]
| + | |
| - | [[Category: Rna-protein complex]]
| + | |
| - | [[Category: Rnp-binding domain]]
| + | |
| - | [[Category: U4/u6 di-snrna]]
| + | |
| - | [[Category: U4/u6 di-snrnp]]
| + | |
| Structural highlights
Function
NH2L1_HUMAN Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nuclear RNA (snRNA), whereas Nop56/58 associate with 15.5K-box C/D small nucleolar RNA complexes. We present structural and biochemical analyses of hPrp31-15.5K-U4 snRNA complexes that show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity despite relaxed RNA sequence requirements. The Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces. Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation.
Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.,Liu S, Li P, Dybkov O, Nottrott S, Hartmuth K, Luhrmann R, Carlomagno T, Wahl MC Science. 2007 Apr 6;316(5821):115-20. PMID:17412961[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nottrott S, Hartmuth K, Fabrizio P, Urlaub H, Vidovic I, Ficner R, Luhrmann R. Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5' stem-loop of U4 snRNA. EMBO J. 1999 Nov 1;18(21):6119-33. PMID:10545122 doi:10.1093/emboj/18.21.6119
- ↑ Liu S, Li P, Dybkov O, Nottrott S, Hartmuth K, Luhrmann R, Carlomagno T, Wahl MC. Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP. Science. 2007 Apr 6;316(5821):115-20. PMID:17412961 doi:316/5821/115
- ↑ Liu S, Li P, Dybkov O, Nottrott S, Hartmuth K, Luhrmann R, Carlomagno T, Wahl MC. Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP. Science. 2007 Apr 6;316(5821):115-20. PMID:17412961 doi:316/5821/115
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