1yvr: Difference between revisions

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<StructureSection load='1yvr' size='340' side='right'caption='[[1yvr]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='1yvr' size='340' side='right'caption='[[1yvr]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1yvr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YVR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1yvr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YVR FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yvp|1yvp]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yvp|1yvp]]</div></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=1yvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvr OCA], [http://pdbe.org/1yvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yvr RCSB], [http://www.ebi.ac.uk/pdbsum/1yvr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yvr 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=1yvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvr OCA], [https://pdbe.org/1yvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yvr RCSB], [https://www.ebi.ac.uk/pdbsum/1yvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yvr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RO60_XENLA RO60_XENLA]] RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. May stabilize these RNAs from degradation.  May play roles in cilia formation and/or maintenance (By similarity).  
[[https://www.uniprot.org/uniprot/RO60_XENLA RO60_XENLA]] RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. May stabilize these RNAs from degradation.  May play roles in cilia formation and/or maintenance (By similarity).  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 19:33, 3 November 2021

Ro autoantigenRo autoantigen

Structural highlights

1yvr is a 1 chain structure with sequence from African clawed frog. 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

[RO60_XENLA] RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. May stabilize these RNAs from degradation. May play roles in cilia formation and/or maintenance (By similarity).

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

The Ro 60 kDa autoantigen is a major target of the immune response in patients with systemic lupus erythematosus. In vertebrate cells, Ro binds misfolded small RNAs and likely functions in RNA quality control. In eukaryotes and bacteria, Ro also associates with small RNAs called Y RNAs. We present structures of unliganded Ro and Ro complexed with two RNAs at 1.95 and 2.2 A resolution, respectively. Ro consists of a von Willebrand factor A domain and a doughnut-shaped domain composed of HEAT repeats. In the complex, a fragment of Y RNA binds on the outer surface of the HEAT-repeat ring, and single-stranded RNA binds in the toroid hole. Mutagenesis supports a binding site for misfolded RNAs that encompasses both sites, with a single-stranded end inserted into the toroid cavity. Our experiments suggest that one role of Y RNAs may be to regulate access of other RNAs to Ro.

Structural insights into RNA quality control: the Ro autoantigen binds misfolded RNAs via its central cavity.,Stein AJ, Fuchs G, Fu C, Wolin SL, Reinisch KM Cell. 2005 May 20;121(4):529-39. PMID:15907467[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Stein AJ, Fuchs G, Fu C, Wolin SL, Reinisch KM. Structural insights into RNA quality control: the Ro autoantigen binds misfolded RNAs via its central cavity. Cell. 2005 May 20;121(4):529-39. PMID:15907467 doi:http://dx.doi.org/10.1016/j.cell.2005.03.009

1yvr, resolution 1.95Å

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OCA