4PM1
Human transthyretin (TTR) complexed with 16-alpha-bromo-estradiol
Summary for 4PM1
| Entry DOI | 10.2210/pdb4pm1/pdb |
| Related | 3GS0 3GS4 4PME 4PMF |
| Descriptor | Transthyretin, (14beta,16alpha,17alpha)-16-bromoestra-1,3,5(10)-triene-3,17-diol, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | human transthyretin hydrophobic ligand solubilization, thyroid hormone-binding protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted: P02766 |
| Total number of polymer chains | 2 |
| Total formula weight | 28381.41 |
| Authors | Stura, E.A.,Ciccone, L. (deposition date: 2014-05-20, release date: 2014-10-08, Last modification date: 2023-09-27) |
| Primary citation | Ciccone, L.,Tepshi, L.,Nencetti, S.,Stura, E.A. Transthyretin complexes with curcumin and bromo-estradiol: evaluation of solubilizing multicomponent mixtures. N Biotechnol, 32:54-64, 2014 Cited by PubMed Abstract: Crystallographic structure determination of protein-ligand complexes of transthyretin (TTR) has been hindered by the low affinity of many compounds that bind to the central cavity of the tetramer. Because crystallization trials are carried out at protein and ligand concentration that approach the millimolar range, low affinity is less of a problem than the poor solubility of many compounds that have been shown to inhibit amyloid fibril formation. To achieve complete occupancy in co-crystallization experiments, the minimal requirement is one ligand for each of the two sites within the TTR tetramer. Here we present a new strategy for the co-crystallization of TTR using high molecular weight polyethylene glycol instead of high ionic strength precipitants, with ligands solubilized in multicomponent mixtures of compounds. This strategy is applied to the crystallization of TTR complexes with curcumin and 16α-bromo-estradiol. Here we report the crystal structures with these compounds and with the ferulic acid that results from curcumin degradation. PubMed: 25224922DOI: 10.1016/j.nbt.2014.09.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.23 Å) |
Structure validation
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