1fxl: Difference between revisions

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<StructureSection load='1fxl' size='340' side='right'caption='[[1fxl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1fxl' size='340' side='right'caption='[[1fxl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fxl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FXL FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fxl]] 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=1FXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FXL FirstGlance]. <br>
</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=1fxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxl OCA], [https://pdbe.org/1fxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fxl RCSB], [https://www.ebi.ac.uk/pdbsum/1fxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxl ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1fxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxl OCA], [https://pdbe.org/1fxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fxl RCSB], [https://www.ebi.ac.uk/pdbsum/1fxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ELAV4_HUMAN ELAV4_HUMAN]] May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR (By similarity). Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS mRNA.<ref>PMID:7898713</ref> <ref>PMID:10710437</ref>
[https://www.uniprot.org/uniprot/ELAV4_HUMAN ELAV4_HUMAN] May play a role in neuron-specific RNA processing. Protects CDKN1A mRNA from decay by binding to its 3'-UTR (By similarity). Binds to AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS mRNA.<ref>PMID:7898713</ref> <ref>PMID:10710437</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1fxl ConSurf].
</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=1fxl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hu proteins bind to adenosine-uridine (AU)-rich elements (AREs) in the 3' untranslated regions of many short-lived mRNAs, thereby stabilizing them. Here we report the crystal structures of the first two RNA recognition motif (RRM) domains of the HuD protein in complex with an 11-nucleotide fragment of a class I ARE (the c-fos ARE; to 1.8 A), and with an 11-nucleotide fragment of a class II ARE (the tumor necrosis factor alpha ARE; to 2.3 A). These structures reveal a consensus RNA recognition sequence that suggests a preference for pyrimidine-rich sequences and a requirement for a central uracil residue in the clustered AUUUA repeats found in class II AREs. Comparison to structures of other RRM domain-nucleic acid complexes reveals two base recognition pockets in all the structures that interact with bases using residues in conserved ribonucleoprotein motifs and at the C-terminal ends of RRM domains. Different conformations of nucleic acid can be bound by RRM domains by using different combinations of base recognition pockets and multiple RRM domains.
Structural basis for recognition of AU-rich element RNA by the HuD protein.,Wang X, Tanaka Hall TM Nat Struct Biol. 2001 Feb;8(2):141-5. PMID:11175903<ref>PMID:11175903</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fxl" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hall, T M.T]]
[[Category: Hall TMT]]
[[Category: Wang, X]]
[[Category: Wang X]]
[[Category: Au-rich element]]
[[Category: Hud]]
[[Category: Protein-rna complex]]
[[Category: Transcription-rna complex]]
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