2mkk
From Proteopedia
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| - | ''' | + | ==Structural model of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in complex with RNA== |
| + | <StructureSection load='2mkk' size='340' side='right' caption='[[2mkk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mkk]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MKK FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mke|2mke]], [[2mkh|2mkh]], [[2mki|2mki]], [[2mkj|2mkj]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mkk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mkk RCSB], [http://www.ebi.ac.uk/pdbsum/2mkk PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cytoplasmic changes in polyA tail length is a key mechanism of translational control and is implicated in germline development, synaptic plasticity, cellular proliferation, senescence, and cancer progression. The presence of a U-rich cytoplasmic polyadenylation element (CPE) in the 3' untranslated regions (UTRs) of the responding mRNAs gives them the selectivity to be regulated by the CPE-binding (CPEB) family of proteins, which recognizes RNA via the tandem RNA recognition motifs (RRMs). Here we report the solution structures of the tandem RRMs of two human paralogs (CPEB1 and CPEB4) in their free and RNA-bound states. The structures reveal an unprecedented arrangement of RRMs in the free state that undergo an original closure motion upon RNA binding that ensures high fidelity. Structural and functional characterization of the ZZ domain (zinc-binding domain) of CPEB1 suggests a role in both protein-protein and protein-RNA interactions. Together with functional studies, the structures reveal how RNA binding by CPEB proteins leads to an optimal positioning of the N-terminal and ZZ domains at the 3' UTR, which favors the nucleation of the functional ribonucleoprotein complexes for translation regulation. | ||
| - | + | A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins.,Afroz T, Skrisovska L, Belloc E, Guillen-Boixet J, Mendez R, Allain FH Genes Dev. 2014 Jul 1;28(13):1498-514. doi: 10.1101/gad.241133.114. PMID:24990967<ref>PMID:24990967</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Afroz, T.]] | ||
| + | [[Category: Allain, F H.T.]] | ||
| + | [[Category: Belloc, E.]] | ||
| + | [[Category: Boixet, J G.]] | ||
| + | [[Category: Mendez, R.]] | ||
| + | [[Category: Skrisovska, L.]] | ||
| + | [[Category: Cpeb1]] | ||
| + | [[Category: Cytoplasmic polyadenylation]] | ||
| + | [[Category: Protein-rna interaction]] | ||
| + | [[Category: Translation regulation]] | ||
| + | [[Category: Translation regulator-rna complex]] | ||
Revision as of 07:58, 23 July 2014
Structural model of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in complex with RNA
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