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5szw

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NMR solution structure of the RRM1 domain of the post-transcriptional regulator HuR

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Retrieved from "http://52.214.119.220/wiki/index.php/5szw"

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 ==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=''>
+<StructureSection load='5szw' size='340' side='right'caption='[[5szw]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5szw]] is a 1 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=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>
+<table><tr><td colspan='2'>[[5szw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5SZW FirstGlance]. <br>
-</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 HUMAN])</td></tr>
+</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'>[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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5szw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szw OCA], [https://pdbe.org/5szw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5szw RCSB], [https://www.ebi.ac.uk/pdbsum/5szw PDBsum], [https://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>
+[https://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) functions as a major post-transcriptional regulator of gene expression through its RNA-binding activity. HuR is composed by three RNA recognition motifs, namely RRM1, RRM2, and RRM3. The two N-terminal RRM domains are disposed in tandem and contribute mostly to HuR interaction with adenine and uracil-rich elements (ARE) in mRNA. Here, we used a combination of NMR and electrospray ionization-ion mobility spectrometry-mass spectrometry (ESI-IMS-MS) to characterize the structure, dynamics, RNA recognition, and dimerization of HuR RRM1. Our solution structure reveals a canonical RRM fold containing a 19-residue, intrinsically disordered N-terminal extension, which is not involved in RNA binding. NMR titration results confirm the primary RNA-binding site to the two central beta-strands, beta1 and beta3, for a cyclooxygenase 2 (Cox2) ARE I-derived, 7-nucleotide RNA ligand. We show by (15)N relaxation that, in addition to the N- and C-termini, the beta2-beta3 loop undergoes fast backbone dynamics (ps-ns) both in the free and RNA-bound state, indicating that no structural ordering happens upon RNA interaction. ESI-IMS-MS reveals that HuR RRM1 dimerizes, however dimer population represents a minority. Dimerization occurs via the alpha-helical surface, which is oppositely orientated to the RNA-binding beta-sheet. By using a DNA analog of the Cox2 ARE I, we show that DNA binding stabilizes HuR RRM1 monomer and shifts the monomer-dimer equilibrium toward the monomeric species. Altogether, our results deepen the current understanding of the mechanism of RNA recognition employed by HuR.
-Oligomeric transition and dynamics of RNA binding by the HuR RRM1 domain in solution.,Lixa C, Mujo A, de Magalhaes MTQ, Almeida FCL, Lima LMTR, Pinheiro AS J Biomol NMR. 2018 Dec;72(3-4):179-192. doi: 10.1007/s10858-018-0217-y. Epub 2018, Dec 8. PMID:30535889<ref>PMID:30535889</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5szw" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Almeida, F C.L]]
+[[Category: Almeida FCL]]
-[[Category: Jendiroba, K A]]
+[[Category: Jendiroba KA]]
-[[Category: Lima, L M.T R]]
+[[Category: Lima LMTR]]
-[[Category: Lixa, C]]
+[[Category: Lixa C]]
-[[Category: Mujo, A]]
+[[Category: Mujo A]]
-[[Category: Pinheiro, A S]]
+[[Category: Pinheiro AS]]
-[[Category: Rna binding protein]]
-[[Category: Rna-binding protein post-trasncriptional regulation rna recognition motif]]

5szw

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NMR solution structure of the RRM1 domain of the post-transcriptional regulator HuR

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