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5szw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR solution structure of the RRM1 domain of the post-transcriptional regulator HuR== | |
| + | <StructureSection load='5szw' size='340' side='right' caption='[[5szw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5szw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SZW FirstGlance]. <br> | ||
| + | </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=5szw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szw OCA], [http://pdbe.org/5szw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5szw RCSB], [http://www.ebi.ac.uk/pdbsum/5szw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5szw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ELAV1_HUMAN ELAV1_HUMAN]] Involved in 3'-UTR ARE-mediated MYC stabilization. Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, HUR binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro.<ref>PMID:19029303</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human antigen R (HuR) is a ubiquitous protein that recognizes adenylate and uridylate-rich elements in mRNA, thereby interfering with the fate of protein translation. This protein plays a central role in the outcome of the inflammatory response as it may stabilize or silence mRNAs of key components of the immune system. HuR is able to interact with other RNA-binding proteins, reflecting a complex network that dictates mRNAs post-transcriptional control. HuR is composed of three functional domains, known as RNA-recognition motifs (RRM1, RRM2 and RRM3). It is known that RRM1 is the most important domain for mRNA-binding affinity. In this study, we completed the NMR chemical shift assignment of the RRM1 domain of HuR, as a first step to further establishing the structure, dynamics and function relationship for this protein. | ||
| - | + | (1)H, (15)N and (13)C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR.,Mujo A, Lixa C, Carneiro LA, Anobom CD, Almeida FC, Pinheiro AS Biomol NMR Assign. 2015 Oct;9(2):281-4. doi: 10.1007/s12104-014-9592-9. Epub 2014, Dec 9. PMID:25487676<ref>PMID:25487676</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5szw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Almeida, F C.L]] | ||
| + | [[Category: Jendiroba, K A]] | ||
| + | [[Category: Lima, L M.T R]] | ||
[[Category: Lixa, C]] | [[Category: Lixa, C]] | ||
[[Category: Mujo, A]] | [[Category: Mujo, A]] | ||
| - | + | [[Category: Pinheiro, A S]] | |
| - | [[Category: Pinheiro, A | + | [[Category: Rna binding protein]] |
| - | [[Category: | + | [[Category: Rna-binding protein post-trasncriptional regulation rna recognition motif]] |
| - | [[Category: | + | |
Revision as of 09:34, 13 September 2017
NMR solution structure of the RRM1 domain of the post-transcriptional regulator HuR
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