View source for 2my7


==NMR Structure of unfolding intermediate state of RRM-3 domain of ETR-3==
<StructureSection load='2my7' size='340' side='right'caption='[[2my7]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2my7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2mik 2mik]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MY7 FirstGlance]. <br>
</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=2my7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2my7 OCA], [https://pdbe.org/2my7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2my7 RCSB], [https://www.ebi.ac.uk/pdbsum/2my7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2my7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CELF2_HUMAN CELF2_HUMAN] RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre-mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury (By similarity). Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to an intronic RNA element responsible for the silencing of exon 21 splicing (By similarity). Binds to (CUG)n repeats (By similarity).<ref>PMID:11577082</ref> <ref>PMID:11158314</ref> <ref>PMID:11931771</ref> <ref>PMID:12649496</ref> <ref>PMID:14973222</ref> <ref>PMID:15657417</ref> <ref>PMID:15894795</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prevalence of one or more partially folded intermediates during protein unfolding with different secondary and ternary conformations has been identified as an integral character of protein unfolding. These transition-state species need to be characterized structurally for elucidation of their folding pathways. We have determined the three-dimensional structure of an intermediate state with increased conformational space sampling under urea-denaturing condition. The protein unfolds completely at 10 M urea but retains residual secondary structural propensities with restricted motion. Here, we describe the native state, observable intermediate state, and unfolded state for ETR-3 RRM-3, which has canonical RRM fold. These observations can shed more light on unfolding events for RRM-containing proteins.

Structure of an Unfolding Intermediate of an RRM Domain of ETR-3 Reveals Its Native-like Fold.,Bhatt H, Ganguly AK, Sharma S, Kushwaha GS, Firoz Khan M, Sen S, Bhavesh NS Biophys J. 2019 Dec 6. pii: S0006-3495(19)34350-4. doi:, 10.1016/j.bpj.2019.11.3392. PMID:31866002<ref>PMID:31866002</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2my7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bhatt HP]]
[[Category: Bhavesh NS]]
[[Category: Ganguly AK]]