5H0V
Crystal structure of H88A mutated human transthyretin
Summary for 5H0V
| Entry DOI | 10.2210/pdb5h0v/pdb |
| Related | 5H0W 5H0X 5H0Y 5H0Z |
| Descriptor | Transthyretin, (4S)-2-METHYL-2,4-PENTANEDIOL, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | transthhyretin, amyloidosis, transporter, transport protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted: P02766 |
| Total number of polymer chains | 4 |
| Total formula weight | 55898.78 |
| Authors | Yokoyama, T.,Hanawa, Y.,Obita, T.,Mizuguchi, M. (deposition date: 2016-10-07, release date: 2017-06-14, Last modification date: 2024-03-20) |
| Primary citation | Yokoyama, T.,Hanawa, Y.,Obita, T.,Mizuguchi, M. Stability and crystal structures of His88 mutant human transthyretins FEBS Lett., 591:1862-1871, 2017 Cited by PubMed Abstract: Destabilization of human transthyretin (TTR) has been implicated in its misfolding and aggregation. A previous study on the neutron crystal structure of TTR suggested that a large hydrogen bond network around H88 which includes water molecules is significantly involved in the stability of wild-type TTR (WT-TTR). Here, we demonstrate that the H88R mutant associated with amyloid cardiomyopathy is substantially destabilized compared with WT-TTR. In order to clarify the role of H88 and the hydrogen bond network in the stability of TTR, we determined the thermodynamic stability and the crystal structure of H88 mutants (H88A, H88F, H88Y, and H88S). Our results suggest that in some cases TTR is destabilized due to alterations in bound water molecules as well as structural changes in TTR itself. PubMed: 28563699DOI: 10.1002/1873-3468.12704 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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