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| | <StructureSection load='1g2e' size='340' side='right'caption='[[1g2e]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1g2e' size='340' side='right'caption='[[1g2e]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1g2e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G2E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1g2e]] 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=1G2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G2E FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fxl|1fxl]]</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]] 2.3Å</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=1g2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2e OCA], [http://pdbe.org/1g2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g2e RCSB], [http://www.ebi.ac.uk/pdbsum/1g2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2e 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=1g2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2e OCA], [https://pdbe.org/1g2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g2e RCSB], [https://www.ebi.ac.uk/pdbsum/1g2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[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]]
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| - | [[Category: Protein-rna complex]]
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| - | [[Category: Transcription-rna complex]]
| + | |
| - | [[Category: Tumor necrosis factor]]
| + | |
| Structural highlights
Function
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.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu J, Dalmau J, Szabo A, Rosenfeld M, Huber J, Furneaux H. Paraneoplastic encephalomyelitis antigens bind to the AU-rich elements of mRNA. Neurology. 1995 Mar;45(3 Pt 1):544-50. PMID:7898713
- ↑ King PH. RNA-binding analyses of HuC and HuD with the VEGF and c-myc 3'-untranslated regions using a novel ELISA-based assay. Nucleic Acids Res. 2000 Apr 1;28(7):E20. PMID:10710437
- ↑ Wang X, Tanaka Hall TM. Structural basis for recognition of AU-rich element RNA by the HuD protein. Nat Struct Biol. 2001 Feb;8(2):141-5. PMID:11175903 doi:10.1038/84131
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