2kfy: Difference between revisions
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<StructureSection load='2kfy' size='340' side='right' caption='[[2kfy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2kfy' size='340' side='right' caption='[[2kfy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kfy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2kfy]] is a 2 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=2KFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KFY FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hgl|2hgl]], [[2kg0|2kg0]], [[2kg1|2kg1]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hgl|2hgl]], [[2kg0|2kg0]], [[2kg1|2kg1]]</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=2kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kfy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kfy RCSB], [http://www.ebi.ac.uk/pdbsum/2kfy PDBsum]</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=2kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kfy OCA], [http://pdbe.org/2kfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kfy RCSB], [http://www.ebi.ac.uk/pdbsum/2kfy PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2kfy" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Allain, F H.T]] | [[Category: Allain, F H.T]] | ||
[[Category: Dominguez, C]] | [[Category: Dominguez, C]] | ||
Revision as of 16:02, 10 September 2015
NMR structure of the first qRRM of hnRNP F in complex with AGGGAU G-tract RNANMR structure of the first qRRM of hnRNP F in complex with AGGGAU G-tract RNA
Structural highlights
Function[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.[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 PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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