View source for 1rgo


==Structural Basis for Recognition of the mRNA Class II AU-Rich Element by the Tandem Zinc Finger Domain of TIS11d==
<StructureSection load='1rgo' size='340' side='right'caption='[[1rgo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rgo]] is a 2 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=1RGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RGO 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1rgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgo OCA], [https://pdbe.org/1rgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rgo RCSB], [https://www.ebi.ac.uk/pdbsum/1rgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rgo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TISD_HUMAN TISD_HUMAN] Probable regulatory protein involved in regulating the response to growth factors. RNA-binding protein that binds to 5'UUAUUUAUUU-3' core sequence. Binds to the class II AU-rich element (ARE) in the 3'-UTR of target mRNAs and promotes their deadenylation and degradation.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/1rgo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1rgo ConSurf].
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== Publication Abstract from PubMed ==
The tandem zinc finger (TZF) domain of the protein TIS11d binds to the class II AU-rich element (ARE) in the 3' untranslated region (3' UTR) of target mRNAs and promotes their deadenylation and degradation. The NMR structure of the TIS11d TZF domain bound to the RNA sequence 5'-UUAUUUAUU-3' comprises a pair of novel CCCH fingers of type CX(8)CX(5)CX(3)H separated by an 18-residue linker. The two TIS11d zinc fingers bind in a symmetrical fashion to adjacent 5'-UAUU-3' subsites on the single-stranded RNA via a combination of electrostatic and hydrogen-bonding interactions, with intercalative stacking between conserved aromatic side chains and the RNA bases. Sequence specificity in RNA recognition is achieved by a network of intermolecular hydrogen bonds, mostly between TIS11d main-chain functional groups and the Watson-Crick edges of the bases. The TIS11d structure provides insights into the RNA-binding functions of this large family of CCCH zinc finger proteins.

Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d.,Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE Nat Struct Mol Biol. 2004 Mar;11(3):257-64. Epub 2004 Feb 8. PMID:14981510<ref>PMID:14981510</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1rgo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Dyson HJ]]
[[Category: Hudson BP]]
[[Category: Martinez-Yamout MA]]
[[Category: Wright PE]]