4L1T
Transthyretin in complex with (E)-3-(dimethylamino)-5-(4-hydroxy-3,5-dimethylstyryl)benzoic acid
Summary for 4L1T
| Entry DOI | 10.2210/pdb4l1t/pdb |
| Related | 3CN0 3CN1 |
| Descriptor | Transthyretin, 3-(dimethylamino)-5-[(E)-2-(4-hydroxy-3,5-dimethylphenyl)ethenyl]benzoic acid (3 entities in total) |
| Functional Keywords | hormone transport protein, thyroxine, retinol, transport protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P02766 |
| Total number of polymer chains | 2 |
| Total formula weight | 28177.47 |
| Authors | Connelly, S.,Wilson, I.A. (deposition date: 2013-06-03, release date: 2013-10-02, Last modification date: 2023-09-20) |
| Primary citation | Baranczak, A.,Connelly, S.,Liu, Y.,Choi, S.,Grimster, N.P.,Powers, E.T.,Wilson, I.A.,Kelly, J.W. Fluorogenic small molecules requiring reaction with a specific protein to create a fluorescent conjugate for biological imaging-what we know and what we need to learn. Biopolymers, 101:484-495, 2014 Cited by PubMed Abstract: We seek fluorogenic small molecules that generate a fluorescent conjugate signal if and only if they react with a given protein-of-interest (i.e., small molecules for which noncovalent binding to the protein-of-interest is insufficient to generate fluorescence). Consequently, it is the new chemical entity afforded by the generally irreversible reaction between the small molecule and the protein-of-interest that enables the energy of an electron occupying the lowest unoccupied molecular orbital (LUMO) of the chromophore to be given off as a photon instead of being dissipated by nonradiative mechanisms in complex biological environments. This category of fluorogenic small molecules is created by starting with environmentally sensitive fluorophores that are modified by an essential functional group that efficiently quenches the fluorescence until a chemoselective reaction between that functional group and the protein-of-interest occurs, yielding the fluorescent conjugate. Fluorogenic small molecules are envisioned to be useful for a wide variety of applications, including live cell imaging without the requirement for washing steps and pulse-chase kinetic analyses of protein synthesis, trafficking, degradation, etc. PubMed: 24105107DOI: 10.1002/bip.22407 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.16 Å) |
Structure validation
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