2i91: Difference between revisions
New page: left|200px<br /><applet load="2i91" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i91, resolution 2.65Å" /> '''60kDa Ro autoantigen... |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:2i91.gif|left|200px]]<br /><applet load="2i91" size=" | [[Image:2i91.gif|left|200px]]<br /><applet load="2i91" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2i91, resolution 2.65Å" /> | caption="2i91, resolution 2.65Å" /> | ||
'''60kDa Ro autoantigen in complex with a fragment of misfolded RNA'''<br /> | '''60kDa Ro autoantigen in complex with a fragment of misfolded RNA'''<br /> | ||
==Overview== | ==Overview== | ||
The Ro autoantigen is ring-shaped, binds misfolded noncoding RNAs and is | The Ro autoantigen is ring-shaped, binds misfolded noncoding RNAs and is proposed to function in quality control. Here we determine how Ro interacts with misfolded RNAs. Binding of Ro to misfolded precursor (pre)-5S ribosomal RNA requires a single-stranded 3' end and helical elements. As mutating most sequences of the helices and tail results in modest decreases in binding, Ro may be able to associate with a range of RNAs. Ro binds several other RNAs that contain single-stranded tails. A crystal structure of Ro bound to a misfolded pre-5S rRNA fragment reveals that the tail inserts into the cavity, while a helix binds on the surface. Most contacts of Ro with the helix are to the backbone. Mutagenesis reveals that Ro has an extensive RNA-binding surface. We propose that Ro uses this surface to scavenge RNAs that fail to bind their specific RNA-binding proteins. | ||
==About this Structure== | ==About this Structure== | ||
2I91 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with ACT and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2I91 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I91 OCA]. | ||
==Reference== | ==Reference== | ||
Line 13: | Line 13: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Reinisch, K | [[Category: Reinisch, K M.]] | ||
[[Category: Stein, A | [[Category: Stein, A J.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: MG]] | [[Category: MG]] | ||
Line 22: | Line 22: | ||
[[Category: von willebrand factor a]] | [[Category: von willebrand factor a]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:13 2008'' |
Revision as of 18:50, 21 February 2008
|
60kDa Ro autoantigen in complex with a fragment of misfolded RNA
OverviewOverview
The Ro autoantigen is ring-shaped, binds misfolded noncoding RNAs and is proposed to function in quality control. Here we determine how Ro interacts with misfolded RNAs. Binding of Ro to misfolded precursor (pre)-5S ribosomal RNA requires a single-stranded 3' end and helical elements. As mutating most sequences of the helices and tail results in modest decreases in binding, Ro may be able to associate with a range of RNAs. Ro binds several other RNAs that contain single-stranded tails. A crystal structure of Ro bound to a misfolded pre-5S rRNA fragment reveals that the tail inserts into the cavity, while a helix binds on the surface. Most contacts of Ro with the helix are to the backbone. Mutagenesis reveals that Ro has an extensive RNA-binding surface. We propose that Ro uses this surface to scavenge RNAs that fail to bind their specific RNA-binding proteins.
About this StructureAbout this Structure
2I91 is a Single protein structure of sequence from Xenopus laevis with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen., Fuchs G, Stein AJ, Fu C, Reinisch KM, Wolin SL, Nat Struct Mol Biol. 2006 Nov;13(11):1002-9. Epub 2006 Oct 15. PMID:17041599
Page seeded by OCA on Thu Feb 21 17:50:13 2008