4kze: Difference between revisions

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kze RCSB], [http://www.ebi.ac.uk/pdbsum/4kze PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kze OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kze RCSB], [http://www.ebi.ac.uk/pdbsum/4kze PDBsum]</span></td></tr>
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== Publication Abstract from PubMed ==
Spinach is an in vitro-selected RNA aptamer that binds a GFP-like ligand and activates its green fluorescence. Spinach is thus an RNA analog of GFP and has potentially widespread applications for in vivo labeling and imaging. We used antibody-assisted crystallography to determine the structures of Spinach both with and without bound fluorophore at 2.2-A and 2.4-A resolution, respectively. Spinach RNA has an elongated structure containing two helical domains separated by an internal bulge that folds into a G-quadruplex motif of unusual topology. The G-quadruplex motif and adjacent nucleotides comprise a partially preformed binding site for the fluorophore. The fluorophore binds in a planar conformation and makes extensive aromatic stacking and hydrogen bond interactions with the RNA. Our findings provide a foundation for structure-based engineering of new fluorophore-binding RNA aptamers.
A G-quadruplex-containing RNA activates fluorescence in a GFP-like fluorophore.,Huang H, Suslov NB, Li NS, Shelke SA, Evans ME, Koldobskaya Y, Rice PA, Piccirilli JA Nat Chem Biol. 2014 Jun 22. doi: 10.1038/nchembio.1561. PMID:24952597<ref>PMID:24952597</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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