4Q9R
Crystal structure of an RNA aptamer bound to trifluoroethyl-ligand analog in complex with Fab
Summary for 4Q9R
| Entry DOI | 10.2210/pdb4q9r/pdb |
| Related | 4KZD 4KZE 4Q9Q |
| Descriptor | Fab BL3-6, HEAVY CHAIN, Fab BL3-6, LIGHT CHAIN, Spinach RNA aptamer, ... (6 entities in total) |
| Functional Keywords | g-quadruplex, fluorescence, fluorophore, rna-immune system complex, rna/immune system |
| Biological source | Mus musculus (mouse) More |
| Total number of polymer chains | 3 |
| Total formula weight | 74679.73 |
| Authors | Huang, H.,Suslov, N.B.,Li, N.-S.,Shelke, S.A.,Evans, M.E.,Koldobskaya, Y.,Rice, P.A.,Piccirilli, J.A. (deposition date: 2014-05-01, release date: 2014-06-18, Last modification date: 2024-11-27) |
| Primary citation | Huang, H.,Suslov, N.B.,Li, N.S.,Shelke, S.A.,Evans, M.E.,Koldobskaya, Y.,Rice, P.A.,Piccirilli, J.A. A G-quadruplex-containing RNA activates fluorescence in a GFP-like fluorophore. Nat.Chem.Biol., 10:686-691, 2014 Cited by PubMed Abstract: 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-Å and 2.4-Å 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. PubMed: 24952597DOI: 10.1038/nchembio.1561 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.12 Å) |
Structure validation
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