5EZP
Human transthyretin (TTR) complexed with 4-hydroxy-chalcone
Summary for 5EZP
| Entry DOI | 10.2210/pdb5ezp/pdb |
| Related | 4I89 4PM1 4PMF 4WNS 5AKS |
| Descriptor | Transthyretin, 4-hydroxy-chalcone, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | human transthyretin (ttr), chalcone, inhibitor complex, new crystal polymorph, transport protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted: P02766 |
| Total number of polymer chains | 8 |
| Total formula weight | 108094.82 |
| Authors | Polsinelli, I.,Nencetti, S.,Shepard, W.E.,Orlandini, E.,Stura, E.A. (deposition date: 2015-11-26, release date: 2016-01-27, Last modification date: 2024-01-10) |
| Primary citation | Polsinelli, I.,Nencetti, S.,Shepard, W.,Ciccone, L.,Orlandini, E.,Stura, E.A. A new crystal form of human transthyretin obtained with a curcumin derived ligand. J.Struct.Biol., 194:8-17, 2016 Cited by PubMed Abstract: Transthyretin (TTR), a 54kDa homotetrameric protein that transports thyroxine (T4), has been associated with clinical cases of TTR amyloidosis for its tendency to aggregate to form fibrils. Many ligands with a potential to inhibit fibril formation have been studied by X-ray crystallography in complex with TTR. Unfortunately, the ligand is often found in ambiguous electron density that is difficult to interpret. The ligand validation statistics suggest over-interpretation, even for the most active compounds like diflunisal. The primary technical reason is its position on a crystallographic 2-fold axis in the most common crystal form. Further investigations with the use of polyethylene glycol (PEG) to crystallize TTR complexes have resulted in a new trigonal polymorph with two tetramers in the asymmetric unit. The ligand used to obtain this new polymorph, 4-hydroxychalcone, is related to curcumin. Here we evaluate this crystal form to understand the contribution it may bring to the study of TTR ligands complexes, which are often asymmetric. PubMed: 26796656DOI: 10.1016/j.jsb.2016.01.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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