8W00
Q108K:K40L:T51V:T53S:Y19W:R58W:L117E mutant of hCRBPII bound to synthetic fluorophore TD-1V
This is a non-PDB format compatible entry.
Summary for 8W00
| Entry DOI | 10.2210/pdb8w00/pdb |
| Descriptor | Retinol-binding protein 2, (2E)-3-{5-[4-(dimethylamino)phenyl]thiophen-2-yl}but-2-enal, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | human cellular retinol binding protein ii, hcrbpii, engineered protein, fluorescent protein, retinol binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 31929.82 |
| Authors | Nossoni, Z.,Bingham, C.R.,Geiger, J.H. (deposition date: 2024-02-13, release date: 2024-04-03, Last modification date: 2024-11-13) |
| Primary citation | Santos, E.M.,Chandra, I.,Assar, Z.,Sheng, W.,Ghanbarpour, A.,Bingham, C.,Vasileiou, C.,Geiger, J.H.,Borhan, B. Regulation of Absorption and Emission in a Protein/Fluorophore Complex. Acs Chem.Biol., 19:1725-1732, 2024 Cited by PubMed Abstract: Human cellular retinol binding protein II (hCRBPII) was used as a protein engineering platform to rationally regulate absorptive and emissive properties of a covalently bound fluorogenic dye. We demonstrate the binding of a thio-dapoxyl analog via formation of a protonated imine between an active site lysine residue and the chromophore's aldehyde. Rational manipulation of the electrostatics of the binding pocket results in a 204 nm shift in absorption and a 131 nm shift in emission. The protein is readily expressed in mammalian systems and binds with exogenously delivered fluorophore as demonstrated by live-cell imaging experiments. PubMed: 39046136DOI: 10.1021/acschembio.4c00125 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.23 Å) |
Structure validation
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