4ed5: Difference between revisions
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==Crystal structure of the two N-terminal RRM domains of HuR complexed with RNA== | |||
=== | <StructureSection load='4ed5' size='340' side='right' caption='[[4ed5]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ed5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ED5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ED5 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ELAVL1, HUR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4ed5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ed5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ed5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ed5 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human RNA-binding protein (HuR), a ubiquitously expressed member of the Hu protein family, plays an important role in mRNA degradation and has been implicated as a key post-transcriptional regulator. HuR contains three RNA-recognition motif (RRM) domains. The two N-terminal tandem RRM domains can selectively bind AU-rich elements (AREs), while the third RRM domain (RRM3) contributes to interactions with the poly-A tail of target mRNA and other ligands. Here, the X-ray structure of two methylated tandem RRM domains (RRM1/2) of HuR in their RNA-free form was solved at 2.9 A resolution. The crystal structure of RRM1/2 complexed with target mRNA was also solved at 2.0 A resolution; comparisons of the two structures show that HuR RRM1/2 undergoes conformational changes upon RNA binding. Fluorescence polarization assays (FPA) were used to study the protein-RNA interactions. Both the structure and the FPA analysis indicated that RRM1 is the primary ARE-binding domain in HuR and that the conformational changes induce subsequent contacts of the RNA substrate with the inter-domain linker and RRM2 which greatly improve the RNA-binding affinity of HuR. | |||
The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding.,Wang H, Zeng F, Liu Q, Liu H, Liu Z, Niu L, Teng M, Li X Acta Crystallogr D Biol Crystallogr. 2013 Mar;69(Pt 3):373-80. doi:, 10.1107/S0907444912047828. Epub 2013 Feb 16. PMID:23519412<ref>PMID:23519412</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
<references | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Li, X | [[Category: Li, X]] | ||
[[Category: Liu, Q | [[Category: Liu, Q]] | ||
[[Category: Niu, L | [[Category: Niu, L]] | ||
[[Category: Teng, M | [[Category: Teng, M]] | ||
[[Category: Wang, H | [[Category: Wang, H]] | ||
[[Category: Zeng, F | [[Category: Zeng, F]] | ||
[[Category: Nucleus]] | [[Category: Nucleus]] | ||
[[Category: Rna binding]] | [[Category: Rna binding]] | ||
[[Category: Rna binding protein-rna complex]] | [[Category: Rna binding protein-rna complex]] | ||
[[Category: Rrm]] | [[Category: Rrm]] | ||
Revision as of 10:44, 21 December 2014
Crystal structure of the two N-terminal RRM domains of HuR complexed with RNA
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