2kg1
From Proteopedia
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==Structure of the third qRRM domain of hnRNP F in complex with a AGGGAU G-tract RNA== | ==Structure of the third qRRM domain of hnRNP F in complex with a AGGGAU G-tract RNA== | ||
| - | <StructureSection load='2kg1' size='340' side='right'caption='[[2kg1 | + | <StructureSection load='2kg1' size='340' side='right'caption='[[2kg1]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2kg1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2kg1]] is a 2 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=2KG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KG1 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </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=2kg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kg1 OCA], [https://pdbe.org/2kg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2kg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kg1 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=2kg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kg1 OCA], [https://pdbe.org/2kg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2kg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kg1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/HNRPF_HUMAN HNRPF_HUMAN] Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state.<ref>PMID:20526337</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=2kg1 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=2kg1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The heterogeneous nuclear ribonucleoprotein (hnRNP) F is involved in the regulation of mRNA metabolism by specifically recognizing G-tract RNA sequences. We have determined the solution structures of the three quasi-RNA-recognition motifs (qRRMs) of hnRNP F in complex with G-tract RNA. These structures show that qRRMs bind RNA in a very unusual manner, with the G-tract 'encaged', making the qRRM a novel RNA binding domain. We defined a consensus signature sequence for qRRMs and identified other human qRRM-containing proteins that also specifically recognize G-tract RNAs. Our structures explain how qRRMs can sequester G-tracts, maintaining them in a single-stranded conformation. We also show that isolated qRRMs of hnRNP F are sufficient to regulate the alternative splicing of the Bcl-x pre-mRNA, suggesting that hnRNP F would act by remodeling RNA secondary and tertiary structures. | ||
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| - | Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs.,Dominguez C, Fisette JF, Chabot B, Allain FH Nat Struct Mol Biol. 2010 Jul;17(7):853-61. Epub 2010 Jun 6. PMID:20526337<ref>PMID:20526337</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2kg1" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Allain | + | [[Category: Allain FHT]] |
| - | [[Category: Dominguez | + | [[Category: Dominguez C]] |
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Current revision
Structure of the third qRRM domain of hnRNP F in complex with a AGGGAU G-tract RNA
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