1p1t

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==NMR Structure of the N-terminal RRM domain of Cleavage stimulation factor 64 KDa subunit==
==NMR Structure of the N-terminal RRM domain of Cleavage stimulation factor 64 KDa subunit==
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<StructureSection load='1p1t' size='340' side='right'caption='[[1p1t]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='1p1t' size='340' side='right'caption='[[1p1t]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1p1t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P1T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1p1t]] 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=1P1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P1T FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CSTF2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</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'>[https://proteopedia.org/fgij/fg.htm?mol=1p1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p1t OCA], [https://pdbe.org/1p1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p1t RCSB], [https://www.ebi.ac.uk/pdbsum/1p1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p1t 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=1p1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p1t OCA], [https://pdbe.org/1p1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p1t RCSB], [https://www.ebi.ac.uk/pdbsum/1p1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p1t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p1t ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p1t ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Vertebrate polyadenylation sites are identified by the AAUAAA signal and by GU-rich sequences downstream of the cleavage site. These are recognized by a heterotrimeric protein complex (CstF) through its 64 kDa subunit (CstF-64); the strength of this interaction affects the efficiency of poly(A) site utilization. We present the structure of the RNA-binding domain of CstF-64 containing an RNA recognition motif (RRM) augmented by N- and C-terminal helices. The C-terminal helix unfolds upon RNA binding and extends into the hinge domain where interactions with factors responsible for assembly of the polyadenylation complex occur. We propose that this conformational change initiates assembly. Consecutive Us are required for a strong CstF-GU interaction and we show how UU dinucleotides are recognized. Contacts outside the UU pocket fine tune the protein-RNA interaction and provide different affinities for distinct GU-rich elements. The protein-RNA interface remains mobile, most likely a requirement to bind many GU-rich sequences and yet discriminate against other RNAs. The structural distinction between sequences that form stable and unstable complexes provides an operational distinction between weakly and strongly processed poly(A) sites.
 
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Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein.,Perez Canadillas JM, Varani G EMBO J. 2003 Jun 2;22(11):2821-30. PMID:12773396<ref>PMID:12773396</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 1p1t" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Perez-Canadillas, J M]]
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[[Category: Perez-Canadillas JM]]
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[[Category: Varani, G]]
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[[Category: Varani G]]
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[[Category: C-terminal helix]]
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[[Category: N-terminal helix]]
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[[Category: Rna binding protein]]
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[[Category: Rna recognition motif]]
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Revision as of 05:52, 17 April 2024

NMR Structure of the N-terminal RRM domain of Cleavage stimulation factor 64 KDa subunit

PDB ID 1p1t

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