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| | ==NMR structure of C-terminal domain of human CstF-64== | | ==NMR structure of C-terminal domain of human CstF-64== |
| - | <StructureSection load='2j8p' size='340' side='right'caption='[[2j8p]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='2j8p' size='340' side='right'caption='[[2j8p]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2j8p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2J8P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2j8p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8P FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p1t|1p1t]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2j8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8p OCA], [http://pdbe.org/2j8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j8p RCSB], [http://www.ebi.ac.uk/pdbsum/2j8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8p 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=2j8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8p OCA], [https://pdbe.org/2j8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8p RCSB], [https://www.ebi.ac.uk/pdbsum/2j8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CSTF2_HUMAN CSTF2_HUMAN] One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity).<ref>PMID:9199325</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Agrawal, S]] | + | [[Category: Agrawal S]] |
| - | [[Category: Baecke, J De]] | + | [[Category: Cheng H]] |
| - | [[Category: Cheng, H]] | + | [[Category: De Baecke J]] |
| - | [[Category: Moore, C]] | + | [[Category: Moore C]] |
| - | [[Category: Perez-Canadillas, J M]] | + | [[Category: Perez-Canadillas JM]] |
| - | [[Category: Qu, X]] | + | [[Category: Qu X]] |
| - | [[Category: Varani, G]] | + | [[Category: Varani G]] |
| - | [[Category: Alternative splicing rna15]]
| + | |
| - | [[Category: Cleavage/polyadenylation]]
| + | |
| - | [[Category: Cstf-64]]
| + | |
| - | [[Category: Mrna processing]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Pcf11]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| Structural highlights
Function
CSTF2_HUMAN One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity).[1]
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
Yeast Rna15 and its vertebrate orthologue CstF-64 play critical roles in mRNA 3 '-end processing and in transcription termination downstream of poly(A) sites. These proteins contain N-terminal domains that recognize the poly(A) site, but little is known about their highly conserved C-terminal regions. Here we show by NMR that the C-terminal domains of CstF-64 and Rna15 fold into a three-helix bundle with an uncommon topological arrangement. The structure defines a cluster of evolutionary conserved yet exposed residues we show to be essential for the interaction between Pcf11 and Rna15. Furthermore, we demonstrate that this interaction is critical for the function of Rna15 in 3 '-end processing but dispensable for transcription termination. The C-terminal domain of the Rna15 homologue Pti1 contains critical sequence alterations within this region that are predicted to prevent Pcf11 interaction, providing an explanation for the distinct functions of these two closely related proteins in the 3 '-end formation of RNA polymerase II transcripts. These results define the role of the C-terminal half of Rna15 and provide insight into the network of protein/protein interactions responsible for assembly of the 3 '-end processing apparatus.
The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3'-end processing.,Qu X, Perez-Canadillas JM, Agrawal S, De Baecke J, Cheng H, Varani G, Moore C J Biol Chem. 2007 Jan 19;282(3):2101-15. Epub 2006 Nov 20. PMID:17116658[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takagaki Y, Manley JL. RNA recognition by the human polyadenylation factor CstF. Mol Cell Biol. 1997 Jul;17(7):3907-14. PMID:9199325
- ↑ Qu X, Perez-Canadillas JM, Agrawal S, De Baecke J, Cheng H, Varani G, Moore C. The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3'-end processing. J Biol Chem. 2007 Jan 19;282(3):2101-15. Epub 2006 Nov 20. PMID:17116658 doi:10.1074/jbc.M609981200
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