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1fxl

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Revision as of 07:09, 24 March 2021

CRYSTAL STRUCTURE OF HUD AND AU-RICH ELEMENT OF THE C-FOS RNA

Structural highlights

1fxl is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fxl"

@@ Line 3: / Line 3: @@
 <StructureSection load='1fxl' size='340' side='right'caption='[[1fxl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FXL FirstGlance]. <br>
+<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>
-</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=1fxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxl OCA], [http://pdbe.org/1fxl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fxl RCSB], [http://www.ebi.ac.uk/pdbsum/1fxl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxl ProSAT]</span></td></tr>
+</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>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1fxl

From Proteopedia

Revision as of 07:09, 24 March 2021

CRYSTAL STRUCTURE OF HUD AND AU-RICH ELEMENT OF THE C-FOS RNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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