3bs9

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(New page: 200px<br /><applet load="3bs9" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bs9, resolution 1.95&Aring;" /> '''X-ray structure of h...)
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[[Image:3bs9.jpg|left|200px]]<br /><applet load="3bs9" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="3bs9, resolution 1.95&Aring;" />
 
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'''X-ray structure of human TIA-1 RRM2'''<br />
 
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==About this Structure==
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==X-ray structure of human TIA-1 RRM2==
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3BS9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=IOD:'>IOD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BS9 OCA].
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<StructureSection load='3bs9' size='340' side='right'caption='[[3bs9]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[3bs9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BS9 FirstGlance]. <br>
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[[Category: Kielkopf, C.L.]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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[[Category: Kumar, A.O.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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[[Category: IOD]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bs9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bs9 OCA], [https://pdbe.org/3bs9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bs9 RCSB], [https://www.ebi.ac.uk/pdbsum/3bs9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bs9 ProSAT]</span></td></tr>
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[[Category: apoptosis]]
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</table>
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[[Category: phosphoprotein]]
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== Function ==
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[[Category: rbd]]
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[https://www.uniprot.org/uniprot/TIA1_HUMAN TIA1_HUMAN] Involved in alternative pre-RNA splicing and regulation of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs). Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis.
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[[Category: rna binding domain]]
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== Evolutionary Conservation ==
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[[Category: rna binding protein]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: rna recognition motif]]
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Check<jmol>
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[[Category: rna splicing]]
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<jmolCheckbox>
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[[Category: rna-binding]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/3bs9_consurf.spt"</scriptWhenChecked>
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[[Category: rrm]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bs9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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T-cell-restricted intracellular antigen-1 (TIA-1) regulates alternative pre-mRNA splicing in the nucleus, and mRNA translation in the cytoplasm, by recognizing uridine-rich sequences of RNAs. As a step towards understanding RNA recognition by this regulatory factor, the X-ray structure of the central RNA recognition motif (RRM2) of human TIA-1 is presented at 1.95A resolution. Comparison with structurally homologous RRM-RNA complexes identifies residues at the RNA interfaces that are conserved in TIA-1-RRM2. The versatile capability of RNP motifs to interact with either proteins or RNA is reinforced by symmetry-related protein-protein interactions mediated by the RNP motifs of TIA-1-RRM2. Importantly, the TIA-1-RRM2 structure reveals the locations of mutations responsible for inhibiting nuclear import. In contrast with previous assumptions, the mutated residues are buried within the hydrophobic interior of the domain, where they would be likely to destabilize the RRM fold rather than directly inhibit RNA binding.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:12:12 2008''
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Structure of the central RNA recognition motif of human TIA-1 at 1.95A resolution.,Kumar AO, Swenson MC, Benning MM, Kielkopf CL Biochem Biophys Res Commun. 2008 Mar 21;367(4):813-9. Epub 2008 Jan 15. PMID:18201561<ref>PMID:18201561</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3bs9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Kielkopf CL]]
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[[Category: Kumar AO]]

Current revision

X-ray structure of human TIA-1 RRM2

PDB ID 3bs9

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